Adaptor Protein Complex mu Subunits
Adaptor Protein Complex 1
Adaptor Protein Complex 2
Adaptor Protein Complex 4
Adaptor Protein Complex Subunits
Adaptor Protein Complex delta Subunits
Adaptor Proteins, Vesicular Transport
Adaptor Protein Complex gamma Subunits
Adaptor Protein Complex beta Subunits
Adaptor Protein Complex alpha Subunits
Adaptor Proteins, Signal Transducing
Monomeric Clathrin Assembly Proteins
GRB2 Adaptor Protein
Shc Signaling Adaptor Proteins
Adaptor Protein Complex sigma Subunits
Molecular Sequence Data
Phosphorylation of the medium chain subunit of the AP-2 adaptor complex does not influence its interaction with the tyrosine based internalisation motif of TGN38. (1/92)Tyrosine based motifs conforming to the consensus YXXphi (where phi represents a bulky hydrophobic residue) have been shown to interact with the medium chain subunit of clathrin adaptor complexes. These medium chains are targets for phosphorylation by a kinase activity associated with clathrin coated vesicles. We have used the clathrin coated vesicle associated kinase activity to specifically phosphorylate a soluble recombinant fusion protein of mu2, the medium chain subunit of the plasma membrane associated adaptor protein complex AP-2. We have tested whether this phosphorylation has any effect on the interaction of mu2 with the tyrosine based motif containing protein, TGN38, that has previously been shown to interact with mu2. Phosphorylation of mu2 was shown to have no significant effect on the in vitro interaction of mu2 with the cytosolic domain of TGN38, indicating that reversible phosphorylation of mu2 does not play a role in regulating its direct interaction with tyrosine based internalisation motifs. In addition, although a casein kinase II-like activity has been shown to be associated with clathrin coated vesicles, we show that mu2 is not phosphorylated by casein kinase II implying that another kinase activity is present in clathrin coated vesicles. Furthermore the kinase activity associated with clathrin coated vesicles was shown to be capable of phosphorylating dynamin 1. Phosphorylation of dynamin 1 has previously been shown to regulate its interaction with other proteins involved in clathrin mediated endocytosis. (+info)
Inhibition of the receptor-binding function of clathrin adaptor protein AP-2 by dominant-negative mutant mu2 subunit and its effects on endocytosis. (2/92)Although interactions between the mu2 subunit of the clathrin adaptor protein complex AP-2 and tyrosine-based internalization motifs have been implicated in the selective recruitment of cargo molecules into coated pits, the functional significance of this interaction for endocytosis of many types of membrane proteins remains unclear. To analyze the function of mu2-receptor interactions, we constructed an epitope-tagged mu2 that incorporates into AP-2 and is targeted to coated pits. Mutational analysis revealed that Asp176 and Trp421 of mu2 are involved in the interaction with internalization motifs of TGN38 and epidermal growth factor (EGF) receptor. Inducible overexpression of mutant mu2, in which these two residues were changed to alanines, resulted in metabolic replacement of endogenous mu2 in AP-2 complexes and complete abrogation of AP-2 interaction with the tyrosine-based internalization motifs. As a consequence, endocytosis of the transferrin receptor was severely impaired. In contrast, internalization of the EGF receptor was not affected. These results demonstrate the potential usefulness of the dominant-interfering approach for functional analysis of the adaptor protein family, and indicate that clathrin-mediated endocytosis may proceed in both a mu2-dependent and -independent manner. (+info)
Mu1B, a novel adaptor medium chain expressed in polarized epithelial cells. (3/92)The apical and basolateral plasma membrane domains of polarized epithelial cells contain distinct sets of integral membrane proteins. Biosynthetic targeting of proteins to the basolateral plasma membrane is mediated by cytosolic tail determinants, many of which resemble signals involved in the rapid endocytosis or lysosomal targeting. Since these signals are recognized by adaptor proteins, we hypothesized that there could be epithelial-specific adaptors involved in polarized sorting. Here, we report the identification of a novel member of the adaptor medium chain family, named mu1B, which is closely related to the previously described mu1A (79% amino acid sequence identity). Northern blotting and in situ hybridization analyses reveal the specific expression of mu1B mRNA in a subset of polarized epithelial and exocrine cells. Yeast two-hybrid analyses show that mu1B is capable of interacting with generic tyrosine-based sorting signals. These observations suggest that mu1B may be involved in protein sorting events specific to polarized cells. (+info)
A novel clathrin adaptor complex mediates basolateral targeting in polarized epithelial cells. (4/92)Although polarized epithelial cells are well known to maintain distinct apical and basolateral plasma membrane domains, the mechanisms responsible for targeting membrane proteins to the apical or basolateral surfaces have remained elusive. We have identified a novel form of the AP-1 clathrin adaptor complex that contains as one of its subunits mu1B, an epithelial cell-specific homolog of the ubiquitously expressed mu1A. LLC-PK1 kidney epithelial cells do not express mu1B and missort many basolateral proteins to the apical surface. Stable expression of mu1B selectively restored basolateral targeting, improved the overall organization of LLC-PK1 monolayers, and had no effect on apical targeting. We conclude that basolateral sorting is mediated by an epithelial cell-specific version of the AP-1 complex containing mu1B. (+info)
mu1A-adaptin-deficient mice: lethality, loss of AP-1 binding and rerouting of mannose 6-phosphate receptors. (5/92)The heterotetrameric AP-1 complex is involved in the formation of clathrin-coated vesicles at the trans-Golgi network (TGN) and interacts with sorting signals in the cytoplasmic tails of cargo molecules. Targeted disruption of the mouse mu1A-adaptin gene causes embryonic lethality at day 13.5. In cells deficient in micro1A-adaptin the remaining AP-1 adaptins do not bind to the TGN. Polarized epithelial cells are the only cells of micro1A-adaptin-deficient embryos that show gamma-adaptin binding to membranes, indicating the formation of an epithelial specific AP-1B complex and demonstrating the absence of additional mu1A homologs. Mannose 6-phosphate receptors are cargo molecules that exit the TGN via AP-1-clathrin-coated vesicles. The steady-state distribution of the mannose 6-phosphate receptors MPR46 and MPR300 in mu1A-deficient cells is shifted to endosomes at the expense of the TGN. MPR46 fails to recycle back from the endosome to the TGN, indicating that AP-1 is required for retrograde endosome to TGN transport of the receptor. (+info)
Interactions of HIV-1 nef with the mu subunits of adaptor protein complexes 1, 2, and 3: role of the dileucine-based sorting motif. (6/92)HIV-1 Nef interacts with cellular adaptor protein (AP) complexes and their medium (mu) subunits. However, the role of the dileucine-based sorting motif within Nef in these interactions has been incompletely characterized. Here, yeast two-hybrid assays indicated that HIV-1 Nef interacted not only with the mu subunits of AP-1 and AP-2, but also with that of AP-3. The interactions with mu1 and mu3 were markedly stronger than the interaction with mu2. Leucine residues of the sorting motif were required for the interactions with mu3 and mu2 and contributed to the interaction with mu1. Confocal immunofluorescence microscopy indicated that Nef, AP-1, and AP-3 (but not AP-2) were concentrated in a juxtanuclear region near the cell center, potentially facilitating interaction between Nef and the mu1 and mu3 subunits. However, leucine residues of the sorting motif were not required for this subcellular localization of Nef. These data suggest that the dileucine motif, required for optimal viral replication, functions through interactions with a variety of AP complexes, including AP-3, potentially by recruiting adaptor complexes to subcellular locations specified by additional determinants in the Nef protein. (+info)
RLIP76, an effector of the GTPase Ral, interacts with the AP2 complex: involvement of the Ral pathway in receptor endocytosis. (7/92)RLIP76 is a modular protein that was identified as a putative effector of Ral, a GTPase activated during Ras signaling. To explore further the contribution of the Ral-RLIP76 pathway to Ras signaling, we have looked for partners of RLIP76. Mu2, the medium chain of the AP2 complex is shown to interact with RLIP76. We show also that in vivo endogenous AP2 and RLIP76 form a complex and that this in vivo interaction is independent of cells being stimulated by a growth factor. Furthermore, RLIP76 differentiates AP2 from AP1 in vivo as RLIP76 differentiates mu2 from mu1 in vitro and in two hybrid assays. We show that activated Ral interferes with both tranferrin receptor endocytosis and epidermal growth factor (EGF) receptor endocytosis in HeLa cells. We propose a model where the Ral-RLIP76 pathway connects signal transduction and endocytosis through interaction on one hand between the Ras-Ral pathway and RLIP, on the other hand between RLIP and proteins belonging to the endocytotic machinery. (+info)
Distinct and redundant functions of mu1 medium chains of the AP-1 clathrin-associated protein complex in the nematode Caenorhabditis elegans. (8/92)In the nematode Caenorhabditis elegans, there exist two micro1 medium chains of the AP-1 clathrin-associated protein complex. Mutations of unc-101, the gene that encodes one of the micro1 chains, cause pleiotropic effects (). In this report, we identified and analyzed the second mu1 chain gene, apm-1. Unlike the mammalian homologs, the two medium chains are expressed ubiquitously throughout development. RNA interference (RNAi) experiments with apm-1 showed that apm-1 and unc-101 were redundant in embryogenesis and in vulval development. Consistent with this, a hybrid protein containing APM-1, when overexpressed, rescued the phenotype of an unc-101 mutant. However, single disruptions of apm-1 or unc-101 have distinct phenotypes, indicating that the two medium chains may have distinct functions. RNAi of any one of the small or large chains of AP-1 complex (sigma1, beta1, or gamma) showed a phenotype identical to that caused by the simultaneous disruption of unc-101 and apm-1, but not that by single disruption of either gene. This suggests that the two medium chains may share large and small chains in the AP-1 complexes. Thus, apm-1 and unc-101 encode two highly related micro1 chains that share redundant and distinct functions within AP-1 clathrin-associated protein complexes of the same tissue. (+info)
Adaptor protein complex mu subunits, also known as AP-μ subunits, are a type of protein that plays a role in the sorting and transport of proteins and lipids within cells. They are part of a larger family of adaptor proteins called AP complexes, which are involved in the formation of vesicles that transport cargo between different compartments within cells. The AP-μ subunits are composed of four different proteins, each with a specific role in the vesicle formation process. These proteins are encoded by genes located on different chromosomes and are highly conserved across different species. Mutations in the genes encoding AP-μ subunits have been associated with a number of human diseases, including a type of inherited lysosomal storage disorder called Chediak-Higashi syndrome. This disorder is characterized by the accumulation of large, abnormal lysosomes within cells, which can lead to a range of symptoms including immune deficiency, bleeding disorders, and neurological problems.
Adaptor Protein Complex 3 (AP-3) is a protein complex that plays a crucial role in the sorting and transport of proteins and lipids within cells. It is composed of four subunits: μ1A, μ1B, μ2A, and μ2B, which are encoded by different genes. AP-3 is involved in the sorting of cargo molecules destined for lysosomes, endosomes, and the plasma membrane. It recognizes specific sorting signals on the cargo molecules and mediates their binding to vesicles that transport them to their final destinations. Mutations in the genes encoding AP-3 subunits have been associated with several human diseases, including Hermansky-Pudlak syndrome, Chediak-Higashi syndrome, and a form of retinitis pigmentosa. These diseases are characterized by defects in the immune system, bleeding disorders, and vision problems, respectively.
Adaptor Protein Complex 1 (AP-1) is a protein complex that plays a crucial role in the sorting and transport of proteins and lipids within cells. It is composed of four subunits: AP-1A, AP-1B, AP-1C, and AP-1D, which are encoded by different genes. AP-1 is involved in the formation of coated vesicles, which are small vesicles that bud off from the plasma membrane and transport cargo to various cellular compartments. AP-1 recognizes specific signals on the cargo proteins and helps to sort them into the correct vesicles for transport. Disruptions in AP-1 function have been linked to a number of human diseases, including neurodegenerative disorders, lysosomal storage diseases, and cancer. Therefore, understanding the role of AP-1 in cellular trafficking is important for developing new treatments for these diseases.
Adaptor Protein Complex 2 (AP-2) is a protein complex that plays a crucial role in the sorting and transport of proteins and lipids within cells. It is composed of four subunits: alpha, beta, mu, and sigma, which together form a heterotetramer. AP-2 is involved in the recognition and sorting of cargo molecules destined for different cellular compartments, such as the plasma membrane, lysosomes, and endosomes. It recognizes specific sorting signals on the cargo molecules, such as tyrosine-based motifs, and binds to them through its alpha and beta subunits. Once bound to the cargo molecule, AP-2 recruits other proteins, such as clathrin, to form a coated pit on the plasma membrane. This coated pit then pinches off to form a vesicle that contains the cargo molecule, which is transported to its final destination within the cell. Disruptions in AP-2 function have been linked to various diseases, including neurodegenerative disorders, lysosomal storage diseases, and cancer.
Adaptor Protein Complex 4 (AP-4) is a protein complex that plays a crucial role in the sorting and transport of proteins and lipids within cells. It is composed of four subunits, each with distinct functions, and is involved in the formation of vesicles that transport cargo from the Golgi apparatus to the plasma membrane or to other organelles within the cell. In the medical field, AP-4 is implicated in several diseases, including neurodegenerative disorders such as Parkinson's disease and Alzheimer's disease, as well as certain types of cancer. Mutations in the genes encoding AP-4 subunits have been linked to these conditions, suggesting that the proper functioning of AP-4 is essential for maintaining cellular health. Additionally, AP-4 has been proposed as a potential therapeutic target for the treatment of these diseases.
Adaptor protein complex subunits are proteins that are involved in the formation and function of adaptor protein complexes. These complexes play a crucial role in various cellular processes, including endocytosis, signal transduction, and vesicle trafficking. Adaptor protein complexes are composed of multiple subunits, each with a specific function. These subunits include adaptor proteins, which link the complexes to other proteins, and protein modules, which mediate specific protein-protein interactions. There are several types of adaptor protein complexes, including the AP-1, AP-2, and AP-3 complexes. These complexes are involved in the recognition and sorting of cargo molecules for transport to different cellular compartments, such as the plasma membrane, endosomes, and lysosomes. Disruptions in the function of adaptor protein complexes can lead to various diseases, including neurodegenerative disorders, lysosomal storage diseases, and immune system disorders. Therefore, understanding the structure and function of adaptor protein complexes is important for the development of new therapeutic strategies for these diseases.
Adaptor protein complex delta subunits are a group of proteins that are involved in the regulation of various cellular processes, including endocytosis, signal transduction, and vesicle trafficking. These proteins are part of a larger family of adaptor protein complexes, which are multi-subunit complexes that play a critical role in the sorting and transport of proteins and lipids within cells. The adaptor protein complex delta subunits are composed of several different proteins, including AP-1, AP-2, and AP-3. These proteins are characterized by the presence of a common set of domains, including a clathrin-binding domain, a membrane-binding domain, and a sorting motif. These domains allow the adaptor protein complex delta subunits to interact with other proteins and lipids within the cell, and to mediate the sorting and transport of specific cargo molecules. In the medical field, the adaptor protein complex delta subunits are of interest because they are involved in the regulation of several important cellular processes, including endocytosis and signal transduction. Mutations in the genes encoding these proteins have been linked to a number of human diseases, including neurodegenerative disorders, immune system disorders, and developmental disorders. As such, understanding the function and regulation of the adaptor protein complex delta subunits is an important area of ongoing research in the medical field.
Adaptor proteins, vesicular transport are a class of proteins that play a crucial role in the process of vesicular transport in cells. These proteins function as molecular adaptors that link cargo molecules to the vesicles that transport them within the cell. In vesicular transport, cargo molecules are packaged into vesicles and transported to their destination within the cell or to other cells. Adaptor proteins help to recognize and bind to specific cargo molecules, and then link them to the vesicles that will transport them. This process is essential for the proper functioning of cells, as it allows for the transport of a wide variety of molecules, including proteins, lipids, and carbohydrates. Adaptor proteins, vesicular transport are involved in a number of different types of vesicular transport, including endocytosis, exocytosis, and intracellular trafficking. They are also involved in the regulation of a number of cellular processes, including signal transduction and the regulation of gene expression. In the medical field, adaptor proteins, vesicular transport are the subject of ongoing research, as they play a critical role in many cellular processes and are involved in a number of diseases and disorders. For example, defects in adaptor proteins have been implicated in a number of neurological disorders, including Alzheimer's disease and Parkinson's disease. Additionally, alterations in the expression or function of adaptor proteins have been linked to a number of cancers, including breast cancer and prostate cancer.
Adaptor protein complex gamma subunits, also known as AP-3 subunits, are a group of proteins that play a crucial role in the sorting and transport of proteins within cells. These subunits are part of a larger protein complex called the adaptor protein complex 3 (AP-3), which is involved in the formation of vesicles that transport specific cargo from the Golgi apparatus to lysosomes or other cellular compartments. The AP-3 complex is composed of four subunits: mu1A, mu1B, sigma2, and mu2A. These subunits interact with each other to form a stable complex that recognizes specific sorting signals on the cargo proteins and mediates their transport to the appropriate cellular compartment. Mutations in the genes encoding AP-3 subunits have been associated with a number of human diseases, including Hermansky-Pudlak syndrome, Chediak-Higashi syndrome, and Griscelli syndrome. These disorders are characterized by defects in the immune system, bleeding disorders, and other abnormalities, and are thought to result from impaired trafficking of specific proteins within cells.
Adaptor protein complex beta subunits are a group of proteins that play a crucial role in the formation and function of adaptor protein complexes (APCs). These complexes are involved in various cellular processes, including endocytosis, signal transduction, and vesicle trafficking. The beta subunits of APCs are characterized by their ability to bind to specific proteins, such as clathrin, and to interact with other components of the APC. They are typically composed of a single membrane-spanning domain and a cytoplasmic tail that contains a number of conserved motifs, including an SH3 domain and a phosphotyrosine-binding domain. In the medical field, defects in the genes encoding adaptor protein complex beta subunits have been linked to a number of diseases, including neurodevelopmental disorders, immunodeficiencies, and cancer. For example, mutations in the APBB1 gene, which encodes the beta-1 subunit of the adaptor protein complex 2 (AP-2), have been associated with the neurodegenerative disorder frontotemporal dementia. Similarly, mutations in the APBB2 gene, which encodes the beta-2 subunit of AP-2, have been linked to the development of certain types of cancer.
Adaptor protein complex (AP) alpha subunits are a group of proteins that play a crucial role in the endocytic pathway of cells. These proteins are part of a larger protein complex called the AP-1 complex, which is involved in the sorting and transport of membrane proteins from the trans-Golgi network to endosomes. The AP-1 complex is composed of four subunits: alpha, beta, mu, and sigma. The alpha subunit is the largest subunit and is responsible for recognizing and binding to specific sorting signals on membrane proteins. There are four different isoforms of the alpha subunit, each of which is specific to a different subset of membrane proteins. The AP-1 complex is essential for the proper functioning of the endocytic pathway, which is responsible for the internalization and recycling of membrane proteins and lipids. Mutations in the genes encoding the AP-1 complex alpha subunits have been linked to a number of human diseases, including Hermansky-Pudlak syndrome and Chediak-Higashi syndrome.
Adaptor proteins, signal transducing are a class of proteins that play a crucial role in transmitting signals from the cell surface to the interior of the cell. These proteins are involved in various cellular processes such as cell growth, differentiation, and apoptosis. Adaptor proteins function as molecular bridges that connect signaling receptors on the cell surface to downstream signaling molecules inside the cell. They are characterized by their ability to bind to both the receptor and the signaling molecule, allowing them to transmit the signal from the receptor to the signaling molecule. There are several types of adaptor proteins, including SH2 domain-containing adaptor proteins, phosphotyrosine-binding (PTB) domain-containing adaptor proteins, and WW domain-containing adaptor proteins. These proteins are involved in a wide range of signaling pathways, including the insulin, growth factor, and cytokine signaling pathways. Disruptions in the function of adaptor proteins can lead to various diseases, including cancer, diabetes, and immune disorders. Therefore, understanding the role of adaptor proteins in signal transduction is important for the development of new therapeutic strategies for these diseases.
Clathrin is a protein that plays a crucial role in the process of endocytosis, which is the process by which cells take in substances from their environment. Clathrin forms a lattice-like structure that surrounds and helps to shape the plasma membrane as it buds inward to form a vesicle. This vesicle then pinches off from the plasma membrane and is transported into the cell, where it can be processed and used by the cell. Clathrin is also involved in the transport of certain molecules within the cell, such as the transport of proteins from the Golgi apparatus to the plasma membrane. In the medical field, clathrin is often studied in relation to diseases such as cancer, where it has been implicated in the formation of abnormal blood vessels and the spread of cancer cells.
Monomeric clathrin assembly proteins (mCAPs) are a group of proteins that play a crucial role in the assembly of clathrin-coated vesicles in the endocytic pathway. Clathrin-coated vesicles are small membrane-bound structures that are involved in the internalization of proteins and other molecules from the cell surface into the cell interior. mCAPs are monomeric proteins that interact with clathrin and other components of the endocytic machinery to promote the assembly of clathrin lattices on the membrane. They are thought to function by stabilizing the clathrin triskelion, which is the basic building block of the clathrin lattice, and by facilitating the assembly of additional triskelia into a lattice. mCAPs are found in a variety of organisms, including humans, and are involved in a wide range of cellular processes, including endocytosis, intracellular trafficking, and signal transduction. Mutations in mCAP genes have been linked to a number of human diseases, including neurodegenerative disorders and immune system disorders.
GRB2 (growth factor receptor-bound protein 2) adaptor protein is a protein that plays a role in cell signaling pathways. It is a member of the Grb2 family of adaptor proteins, which are involved in the transmission of signals from cell surface receptors to intracellular signaling pathways. GRB2 is activated by the binding of growth factors or other signaling molecules to cell surface receptors, and it then interacts with other proteins to transmit the signal to downstream signaling pathways. GRB2 is involved in a variety of cellular processes, including cell proliferation, differentiation, and migration. It has been implicated in the development of certain types of cancer, and it is a target for cancer therapy.
SHC (Src Homology and Collagen) signaling adaptor proteins are a family of proteins that play a crucial role in cellular signaling pathways. These proteins are involved in the regulation of cell growth, differentiation, survival, and migration. SHC proteins contain several domains, including an SH2 domain, a SH3 domain, and a tyrosine kinase domain. The SH2 domain allows SHC proteins to bind to phosphorylated tyrosine residues on other proteins, while the SH3 domain mediates interactions with other proteins. The tyrosine kinase domain is inactive in most SHC proteins, but it can become activated in response to certain stimuli, leading to the phosphorylation of other proteins and the activation of downstream signaling pathways. SHC signaling adaptor proteins are involved in a variety of cellular processes, including the regulation of the insulin and insulin-like growth factor (IGF) signaling pathways, the control of cell proliferation and differentiation, and the regulation of cell migration and invasion. Dysregulation of SHC signaling has been implicated in a number of diseases, including cancer, cardiovascular disease, and neurodegenerative disorders.
Adaptor protein complex sigma subunits, also known as AP-σ subunits, are a group of proteins that play a role in the sorting and transport of proteins and lipids within cells. They are part of a larger family of adaptor protein complexes, which are involved in the formation of vesicles that transport cargo between different compartments within cells. The AP-σ subunits are specifically involved in the formation of vesicles that bud from the trans-Golgi network (TGN) and transport cargo to the plasma membrane. They are thought to play a role in the sorting of specific proteins and lipids for transport to the plasma membrane, and they may also be involved in the regulation of membrane trafficking. In the medical field, the AP-σ subunits are of interest because they have been implicated in a number of diseases, including neurodegenerative disorders such as Alzheimer's disease and Parkinson's disease. Mutations in genes encoding AP-σ subunits have been linked to these conditions, and it is thought that dysfunction of the AP-σ complex may contribute to the development of these diseases.
In the medical field, a protein subunit refers to a smaller, functional unit of a larger protein complex. Proteins are made up of chains of amino acids, and these chains can fold into complex three-dimensional structures that perform a wide range of functions in the body. Protein subunits are often formed when two or more protein chains come together to form a larger complex. These subunits can be identical or different, and they can interact with each other in various ways to perform specific functions. For example, the protein hemoglobin, which carries oxygen in red blood cells, is made up of four subunits: two alpha chains and two beta chains. Each of these subunits has a specific structure and function, and they work together to form a functional hemoglobin molecule. In the medical field, understanding the structure and function of protein subunits is important for developing treatments for a wide range of diseases and conditions, including cancer, neurological disorders, and infectious diseases.
Coated vesicles are small membrane-bound sacs that are involved in the transport of molecules within cells. They are coated with a layer of proteins, called clathrin, which helps to regulate the movement of molecules into and out of the vesicle. Coated vesicles are involved in a variety of cellular processes, including the transport of proteins from the endoplasmic reticulum to the Golgi apparatus, the transport of lipids and other molecules between organelles, and the transport of molecules to the plasma membrane for secretion or uptake. In the medical field, coated vesicles are often studied in the context of diseases such as neurodegenerative disorders, where the abnormal accumulation of coated vesicles has been observed.
In the medical field, an amino acid sequence refers to the linear order of amino acids in a protein molecule. Proteins are made up of chains of amino acids, and the specific sequence of these amino acids determines the protein's structure and function. The amino acid sequence is determined by the genetic code, which is a set of rules that specifies how the sequence of nucleotides in DNA is translated into the sequence of amino acids in a protein. Each amino acid is represented by a three-letter code, and the sequence of these codes is the amino acid sequence of the protein. The amino acid sequence is important because it determines the protein's three-dimensional structure, which in turn determines its function. Small changes in the amino acid sequence can have significant effects on the protein's structure and function, and this can lead to diseases or disorders. For example, mutations in the amino acid sequence of a protein involved in blood clotting can lead to bleeding disorders.
Adaptor-related protein complex 2, alpha 1
Adaptor complexes medium subunit domain
Clathrin adaptor protein
List of adaptins
Beta2-adaptin C-terminal domain
Vesicular transport adaptor protein
AP2 adaptor complex
Interleukin-1 receptor family
List of MeSH codes (D12.776.543)
Allograft inflammatory factor 1
SGN Unigene - Show All Stored BLAST Hits - Sol Genomics Network
AP1M2 Gene - Wiki-Pi
KNOP1 and AP2M1 - Wiki-MPM
ap1m1 | ZMP | Busch Lab
MedlinePlus: Genes: O
OT 16G00570.1 details
Human SPTLC3(Serine Palmitoyltransferase, Long Chain Base Subunit 3) ELISA Kit - Elisa kits Gentaur
Endocytosis in the adaptation to cellular stress
NEW (2008) DeCS DESCRIPTORS WITH SCOPE NOTES (UNIT RECORD FORMAT; 21/02/2008
NEW (2008) DeCS DESCRIPTORS WITH SCOPE NOTES (UNIT RECORD FORMAT; 21/02/2008
NEW (2008) DeCS DESCRIPTORS WITH SCOPE NOTES (UNIT RECORD FORMAT; 21/02/2008
NEW (2008) DeCS DESCRIPTORS WITH SCOPE NOTES (UNIT RECORD FORMAT; 21/02/2008
A late-stage assembly checkpoint of the human mitochondrial ribosome large subunit | Nature Communications
Mouse CD163(Cluster Of Differentiation) ELISA Kit - Lotuskring Poeldijk
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GSE17721 POLYIC VS CPG 8H BMDC DN
6.4 Development of retinal ganglion cell dendritic structure and synaptic connections. by Ning Tian - Webvision
IJMS | Free Full-Text | Possible Pathogenesis and Prevention of Long COVID: SARS-CoV-2-Induced Mitochondrial Disorder
Database Name: GTEx Human Nerve - Tibial Apr14 RPKM
Comparison of the transcriptome in circulating leukocytes in early lactation between primiparous and multiparous cows provides...
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The Jena Protein-Protein Interaction Website (PPI): Selected Publications
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Cyclins | Profiles RNS
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MH DELETED MN ADDED MN
Mitochondrial ribosomal proteins1
- Differentially expressed candidate genes for ageing previously identified in the human blood transcriptome up-regulated in PP cows were mainly associated with T-cell function ( CCR7 , CD27 , IL7R , CAMK4 , CD28 ), mitochondrial ribosomal proteins ( MRPS27 , MRPS9 , MRPS31 ), and DNA replication and repair ( WRN ). (biomedcentral.com)
- The plasma membrane can be envisioned as a central compartment in the cellular adaptation to diverse stress conditions as it shapes the interactions between cells and their environment by harboring an elaborate complement of transmembrane proteins, e.g. transporters, channels, receptors, or adhesion proteins. (cell-stress.com)
- ATP synthase F1 subunit beta [Source:HG. (gsea-msigdb.org)
- Proteins synthesized at the ER are subject to covalent modifications that include N- and O-glycosylation, disulfide bond formation, and in some cases, proline and lysine hydroxylation. (stanford.edu)
- This highly complex 'protein biogenesis' process is assisted by a diverse network of folding catalysts and protein-modifying enzymes and is scrutinized by molecular chaperones and other 'quality control' factors which ensure that only correctly folded and assembled proteins exit the ER and proceed to distal compartments of the secretory pathway. (stanford.edu)
- The plasma membrane is not only the first point of encounter for many types of environmental stress, but given the diversity of receptor proteins and their associated molecules also represents the site at which many cellular signal cascades originate. (cell-stress.com)
- Deciphering soluble and membrane protein function using yeast systems. (leibniz-fli.de)
- Membrane proteins must be threaded co-translocationally into the lipid bilayer to become membrane-integrated, often with complex topologies and typically form hetero- or homo- oligomers. (stanford.edu)
- Structural basis of BAM-mediated outer membrane β-barrel protein assembly. (ucsf.edu)
- The vast majority of proteins entering the secretory pathway are synthesized on ribosomes docked at ER translocons and are co-transationally translocated into the ER lumen. (stanford.edu)
- Triangle network motifs predict complexes by complementing high-error interactomes with structural information. (leibniz-fli.de)
- The corresponding gene, AtWRINKLED1 ( AtWRI1, At3g54320), encodes a protein with two APETALA2-ethylene responsive element-binding protein (AP2/EREBP) motifs that is a signature for plant-specific transcription factors involved in a wide range of developmental processes [ 5 , 6 ]. (biomedcentral.com)
- RESEARCH positive bacteria that contain accessory pilus proteins, that primers sipA_up and sipA_dn (Table 1) designed against serve as adhesins ( 15 - 17 ) or adaptors for pilus attachment the PI-2-specifi c gene sipA . (cdc.gov)
- While RNA makes up most of the composition of bacterial and cytosolic eukaryotic ribosomes, mammalian mitochondrial ribosomes present a more elaborate protein shell, which aids coping with the oxidative microenvironment. (nature.com)
- These cell surface proteins impinge on the vast majority of all cellular functions by mediating nutrient uptake, preserving ion homeostasis and initiating complex signaling cascades in response to extracellular cues. (cell-stress.com)
- Ligand and G-protein selectivity in the κ-opioid receptor. (ucsf.edu)
- However, these proteins are conserved not only in multiple ETEC isolates, but also in commensal bacteria. (biomedcentral.com)
- These assist with protein folding and, thereby, help to keep the cellular protein machinery functional in spite of adverse thermal conditions. (cell-stress.com)
- GA binding protein transcription factor. (gsea-msigdb.org)
- MipA is an immunoreactive protein [ 6 ] that belongs to a family of proteins involved in remodeling peptidoglycan. (biomedcentral.com)
- clathrin assembly protein complex 1, me. (cornell.edu)
- While the RNA components of the mitoribosome are mitochondrially-encoded, all MRPs and assembly factors are encoded in the nuclear genome, thus requiring coordination between two genomes for the assembly of these macromolecular complexes. (nature.com)
- Continued development of an empirical function for predicting and rationalizing protein-protein binding affinities. (leibniz-fli.de)
- Our goal is to elucidate the functional networks that coordinate protein synthesis and quality control in the early secretory pathway. (stanford.edu)
- Here, a genome-wide analysis of the human mitochondrial transcriptome shows that 2'- O -methylation is limited to residues of the mitoribosomal large subunit (mtLSU) 16S mt-rRNA, introduced by MRM1, MRM2 and MRM3, with the modifications installed by the latter two proteins being interdependent. (nature.com)
- Structural basis of mitochondrial protein import by the TIM23 complex. (ucsf.edu)
- The ER is the 'port of entry' for proteins destined for the cell surface and beyond. (stanford.edu)
- Similar to other systems, the mitochondrial ribosome is composed of a small (mtSSU) and a large (mtLSU) subunit, with their core rRNAs, 12S and 16S mitochondrial (mt-) rRNAs, respectively, surrounded by MRPs (30 for the mtSSU and 52 for the mtLSU). (nature.com)
- IFAwith anti-MSP1 antibody showed no overlap in staining betweenMSP1 and Pfμ1 (A). Similar results were seen with antibodies to EBA175 (B). Importantly, anti-RAP1 and anti-Clag3.1 showed co-localization with the Pfμ1-GFP chimeric protein (C and D), suggesting a potential role for Pfμ1 in rhoptry trafficking. (huji.ac.il)
- Redox potentials of uranyl ions in macrocyclic complexes: Quantifying the role of counter-ions. (ucsf.edu)
- Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Human Serine Palmitoyltransferase, Long Chain Base Subunit 3 (SPTLC3) in tissue homogenates, cell lysates and other biological fluids. (1elisakits.com)
- Description: Enzyme-linked immunosorbent assay based on the Double-antibody Sandwich method for detection of Human Serine Palmitoyltransferase, Long Chain Base Subunit 3 (SPTLC3) in samples from tissue homogenates, cell lysates and other biological fluids with no significant corss-reactivity with analogues from other species. (1elisakits.com)
- Description: A sandwich ELISA kit for detection of Serine Palmitoyltransferase, Long Chain Base Subunit 3 from Human in samples from blood, serum, plasma, cell culture fluid and other biological fluids. (1elisakits.com)
- Network properties of complex human disease genes identified through genome-wide association studies. (leibniz-fli.de)
- While the impact of inactivated viral vaccines and live-attenuated bacterial vaccines on the host microbiota have been examined, the potential impact of using subunit vaccines consisting of antigens that are also encoded by commensal organisms has not been investigated. (biomedcentral.com)
- Description: A sandwich quantitative ELISA assay kit for detection of Mouse Serine Palmitoyltransferase, Long Chain Base Subunit 3 (SPTLC3) in samples from tissue homogenates, cell lysates or other biological fluids. (1elisakits.com)
- Small molecule protein-protein interaction inhibitors as CNS therapeutic agents: current progress and future hurdles. (leibniz-fli.de)
- In this case the impaired protein folding induced by heat stress is, at least partially, counteracted by an increased expression of chaperone proteins. (cell-stress.com)
- Discovery and optimization of chromenotriazolopyrimidines as potent inhibitors of the mouse double minute 2-tumor protein 53 protein-protein interaction. (leibniz-fli.de)
- Systems biology: untangling the protein web. (leibniz-fli.de)