The C2A domain of synaptotagmin-like protein 3 (Slp3) is an atypical calcium-dependent phospholipid-binding machine: comparison with the C2A domain of synaptota
TY - JOUR. T1 - Rab family small GTPases-mediated regulation of intracellular logistics in neural development. AU - Shikanai, Mima. AU - Yuzaki, Michisuke. AU - Kawauchi, Takeshi. PY - 2018/8/1. Y1 - 2018/8/1. N2 - Rab family small GTPases play essential roles in various cellular events via the regulation of intracellular logistics comprising a large number of membrane traffic pathways. Emerging evidence reveals the physiological roles of Rab proteins in several tissues, including developing brains. Many Rab proteins, such as Rab5, Rab6, Rab7, Rab8, Rab10, Rab11, Rab17 and Rab18, are shown to regulate neurite outgrowth in PC12 cells and/or axon and dendrite formation in primary cultured neurons. Recent studies have also revealed in vivo roles of several Rab family small GTPases in brain development and its related neurological disorders. In this review, we introduce the physiological function of Rab family proteins in neural development with particular focus on neurite outgrowth and neuronal ...
Rab27 is a member of the Rab subfamily of Ras GTPase proteins. Rab27 protein is membrane-bound and is post-translationally modified by the addition of geranylgeranyl groups on two C-terminal cysteines. Two isoforms of Rab27 are known, encoded by the RAB27A and RAB27B genes. Rab27A and Rab27B were found to control different steps of the exosome secretion pathway. Rab27 proteins are involved in melanosome transport in melanocytes and in killing activity in cytotoxic T lymphocytes. In addition, they have been suggested to play roles in protein transport and small GTPase-mediated signal transduction. Mutations in the RAB27A gene are associated with Griscelli syndrome type 2, a disease characterized by hypopigmentation and immunodeficiency. Rab27A is also known as RAB27A, member RAS oncogene family; GTP-binding protein Ram, RAB27, GS2, RAM, and HsT18676. Rab27B is also known as RAB27B, member RAS oncogene family; and C25KG2.. ...
Rab27 is a member of the Rab subfamily of Ras GTPase proteins. Rab27 protein is membrane-bound and is post-translationally modified by the addition of geranylgeranyl groups on two C-terminal cysteines. Two isoforms of Rab27 are known, encoded by the RAB27A and RAB27B genes. Rab27A and Rab27B were found to control different steps of the exosome secretion pathway. Rab27 proteins are involved in melanosome transport in melanocytes and in killing activity in cytotoxic T lymphocytes. In addition, they have been suggested to play roles in protein transport and small GTPase-mediated signal transduction. Mutations in the RAB27A gene are associated with Griscelli syndrome type 2, a disease characterized by hypopigmentation and immunodeficiency. Rab27A is also known as RAB27A, member RAS oncogene family; GTP-binding protein Ram, RAB27, GS2, RAM, and HsT18676. Rab27B is also known as RAB27B, member RAS oncogene family; and C25KG2.. ...
Rab guanosine triphosphatases (GTPases) regulate vesicle trafficking in eukaryotic cells by reversibly associating with lipid membranes. Inactive Rab GTPases are maintained in the cytosol by binding to GDP-dissociation inhibitor (GDI). It is believed that specialized proteins are required to displace GDI from Rab GTPases before Rab activation by guanosine diphosphate-guanosine 5′-triphosphate (GDP-GTP) exchange factors (GEFs). Here, we found that SidM from Legionella pneumophila could act as both GEF and GDI-displacement factor (GDF) for Rab1. Rab1 released from GDI was inserted into liposomal membranes and was used as a substrate for SidM-mediated nucleotide exchange. During host cell infection, recruitment of Rab1 to Legionella-containing vacuoles depended on the GDF activity of SidM. Thus, GDF and GEF activity can be promoted by a single protein, and GDF activity can coordinate Rab1 recruitment from the GDI-bound pool.. ...
Rab GTPases and their effectors facilitate vesicular transport by tethering donor vesicles to their respective target membranes. Rab9 mediates late endosome to trans-Golgi transport and has recently been found to be a key cellular component for human immunodeficiency virus-1, Ebola, Marburg, and measles virus replication, suggesting that it may be a novel target in the development of broad spectrum antiviral drugs. As part of our structure-based drug design program, we have determined the crystal structure of a C-terminally truncated human Rab9 (residues 1-177) to 1.25-A resolution. The overall structure shows a characteristic nucleotide binding fold consisting of a six-stranded beta-sheet surrounded by five alpha-helices with a tightly bound GDP molecule in the active site. Structure-based sequence alignment of Rab9 with other Rab proteins reveals that its active site consists of residues highly conserved in the Rab GTPase family, implying a common catalytic mechanism. However, Rab9 contains ...
Rab effectors, defined as proteins that interact specifically with the GTP-bound from of a Rab GTPase, come in many flavours and include molecular tethers, fusion regulators, motors, sorting adaptors, kinases, phosphatases, components of membrane contact sites and Rab regulators (Gillingham et al., 2014). The recruitment of such effectors in a spatiotemporally controlled manner contributes strongly to the fidelity and specificity of intracellular membrane traffic. There are also a few examples of proteins that are regulated by GDP-bound Rabs or that interact with Rabs in a nucleotide-independent fashion, including the interactions between Rab21 and β1-integrin, Rab11 and protrudin, Rab7 and VPS34, and Rab27a and Coronin3 (Kimura et al., 2008; Pellinen et al., 2006; Shirane and Nakayama, 2006; Stein et al., 2003); however, the term effector should be reserved for those proteins that interact exclusively with the GTP-bound form of a Rab GTPase. In some cases, different Rab GTPases bind to ...
Rab proteins are small GTPases that play important roles in transport of vesicle cargo and recruitment, association of motor and other proteins with vesicles, and docking and fusion of vesicles at defined locations. In vertebrates, ,75 Rab genes have been identified, some of which have been intensively studied for their roles in endosome and synaptic vesicle trafficking. Recent studies of the functions of certain Rab proteins have revealed specific roles in mediating developmental signal transduction. We have begun a systematic genetic study of the 33 Rab genes in Drosophila. Most of the fly proteins are clearly related to specific vertebrate proteins. We report here the creation of a set of transgenic fly lines that allow spatially and temporally regulated expression of Drosophila Rab proteins. We generated fluorescent protein-tagged wild-type, dominant-negative, and constitutively active forms of 31 Drosophila Rab proteins. We describe Drosophila Rab expression patterns during embryogenesis, ...
The Federal Information Processing Standard (FIPS) Publication 140-3 was a proposed update to the U.S. government computer security standard used to accredit cryptographic modules. The title of the standard is Security Requirements for Cryptographic Modules and FIPS 140-2 remains the currently approved version. Efforts to update FIPS 140-2 date back to the early 2000s. The FIPS 140-3 (2013 Draft) was scheduled for signature by the Secretary of Commerce in August 2013, however that never happened and the draft was subsequently abandoned. In 2014, NIST released a substantially different draft of FIPS 140-3, this version effectively directing the use of an International Organization for Standardization/International Electrotechnical Commission (ISO/IEC) standard, 19790:2012, as the replacement for FIPS 140-2. The 2014 draft of FIPS 140-3 was also abandoned. On August 12, 2015, NIST formally released a statement on the Federal Register asking for comments on the potential use of portions of ISO/IEC ...
Rab GTPases are implicated in endosome-to-plasma membrane recycling, but how such membrane traffic regulators control vascular endothelial growth factor receptor 2 (VEGFR2/KDR) dynamics and function are not well understood. Here, we evaluated two different recycling Rab GTPases, Rab4a and Rab11a, in regulating endothelial VEGFR2 trafficking and signalling with implications for endothelial cell migration, proliferation and angiogenesis. In primary endothelial cells, VEGFR2 displays co-localisation with Rab4a, but not Rab11a GTPase, on early endosomes. Expression of a guanosine diphosphate (GDP)-bound Rab4a S22N mutant caused increased VEGFR2 accumulation in endosomes. TfR and VEGFR2 exhibited differences in endosome-to-plasma membrane recycling in the presence of chloroquine. Depletion of Rab4a, but not Rab11a, levels stimulated VEGF-A-dependent intracellular signalling. However, depletion of either Rab4a or Rab11a levels inhibited VEGF-A-stimulated endothelial cell migration. Interestingly, depletion of
Rab GTPase family 3 contains Rab3A, Rab3B, Rab3C and Rab3D. The Rab3 subfamily contains Rab3A, Rab3B, Rab3C, and Rab3D. All four isoforms were found in mouse brain and endocrine tissues, with varying levels of expression. Rab3A, Rab3B, and Rab3C localized to synaptic and secretory vesicles; Rab3D was expressed at high levels only in adipose tissue, exocrine glands, and the endocrine pituitary, where it is localized to cytoplasmic secretory granules. Rab3 appears to control Ca2+-regulated exocytosis. The appropriate GDP/GTP exchange cycle of Rab3A is required for Ca2+-regulated exocytosis to occur, and interaction of the GTP-bound form of Rab3A with effector molecule(s) is widely believed to be essential for this process. Functionally, most studies point toward a role for Rab3 in the secretion of hormones and neurotransmitters. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with ...
Rab GTPases are key master regulators of membrane maturation and trafficking throughout the endomembrane system of eukaryotic cells. The function of Rab GTPases...
antibody-antibodies.com is the marketplace for research antibodies. Find the right antibody for your research needs. Deregulation of Rab and Rab Effector Genes in Bladder Cancer
The available database information concerning Rab17 and its interactors is insufficient to infer potential effectors and pathways through which this GTPase acts to suppress cancer invasiveness and progression. We, therefore, determined the Rab17 interactome and its influence on the cellular proteome in an unbiased manner. The use of high-accuracy MS-based approaches has enabled us to do this and to show that Rab17 has a close physical and functional relationship with the SNARE protein Vamp8. Rab GTPases are known to recruit specific effector proteins that bind to SNAREs, giving specificity to vesicle fusion (Angers and Merz, 2011). Nevertheless, to our knowledge, our study is the first to provide an indication that the stability and cellular levels of a SNARE protein may be controlled by a Rab GTPase. Moreover, because Vamp8 is the only component of the proteome that is significantly altered following Rab17 knockdown, the relationship between this GTPase and Vamp8 stability is likely to be ...
Rab GTPases define the vesicle trafficking pathways underpinning cell polarization and migration. Here, we find that Rab4, Rab11, and Rab14 and the candidate Rab GDP-GTP exchange factors (GEFs) FAM116A and AVL9 are required for cell migration. Rab14 and its GEF FAM116A localize to and act on an intermediate compartment of the transferrin-recycling pathway prior to Rab11 and after Rab5 and Rab4. This Rab14 intermediate recycling compartment has specific functions in migrating cells discrete from early and recycling endosomes. Rab14-depleted cells show increased N-cadherin levels at junctional complexes and cannot resolve cell-cell junctions. This is due to decreased shedding of cell-surface N-cadherin by the ADAM family protease ADAM10/Kuzbanian. In FAM116A- and Rab14-depleted cells, ADAM10 accumulates in a transferrin-positive endocytic compartment, and the cell-surface level of ADAM10 is correspondingly reduced. FAM116 and Rab14 therefore define an endocytic recycling pathway needed for ADAM protease
The monomeric small GTPase Rab27a is specifically localized on both secretory granules and lysosome-related organelles. Although natural mutations of the Rab27a gene in human Griscelli syndrome and in ashen mice cause partial albinism and immunodeficiency reflecting the dysfunction of lysosome-related organelles, phenotypes resulting from the defective exocytosis of secretory granules have not been reported. To explore the roles of Rab27a in secretory granules, we analyzed insulin secretion profiles in ashen mice. Ashen mice showed glucose intolerance after a glucose load without signs of insulin resistance in peripheral tissues or insulin deficiency in the pancreas. Insulin secretion from isolated islets was decreased specifically in response to high glucose concentrations but not other nonphysiological secretagogues such as high K+ concentrations, forskolin, or phorbol ester. Neither the intracellular Ca2+ concentration nor the dynamics of fusion pore opening after glucose stimulation were ...
Herein, we provide evidence for a Rab-dependent mechanism for regulating VEGFR2 trafficking and signaling from endosomes in primary endothelial cells. Manipulation of GTPase activity through overexpression of GFP-tagged wild-type or mutant Rab7a proteins perturbed endothelial VEGFR2 trafficking, degradation, and signaling. Intriguingly, Rab7a depletion decreased VEGFR2 tyrosine autophosphorylation on residue Y1175, a characteristic signature in VEGFR2-mediated activation and signaling.32 This correlated with ≈50% decrease in VEGF-A-stimulated endothelial cell migration after Rab7a depletion, suggesting a requirement for Rab7a in VEGFR2-mediated signaling. However, in Rab7a-depleted cells, there was increased p42/44 MAPK levels 30 minutes after VEGF-A addition, suggesting increased signaling through this arm of the pathway. A likely explanation is that VEGFR2-regulated signaling to p42/p44 MAPK occurs at the early endosome and is prolonged in Rab7a-depleted cells as VEGFR2 cannot progress ...
This thesis work describes the role of Rab proteins in amyloid processing and clearance in different cell pathways. It also describes an experimental approach used to analyze the expression effects of Rab10 in amyloid beta production. Since the main theory behind neurodegeneration in Alzheimers disease claims that high levels of amyloid beta 42 (Aβ42) molecules trigger widespread neuronal death, control of Aβ42 has been a main target in Alzheimers disease research. In addition, several studies show increased levels of particular Rab proteins in Alzheimers pathogenesis. However, no review consolidates current findings in neurodegeneration of Alzheimers with Rab protein dysfunction. The first chapter of this thesis aims to address this need by providing a current review of Rab proteins associated with APP and neurodegeneration. The second chapter constitutes an experimental approach used to characterize the effects of Rab10 and Sar1A GTPases in APP and amyloid processing. We found that Rab10
The Goldenring laboratory studies a number of subjects that apply broadly to epithelial biology. We pursue three distinct programmatic areas. First, we are investigating the protein machinery required for the regulation of the recycling to the plasma membrane of receptors, ion transporters and ion channels. These studies focus on the ability of the Rab11 family of small GTPases (Rab11a, Rab11b and Rab25) to initiate and coordinate the assembly of multiprotein complexes regulating vesicle trafficking. Over the past several years, we have identified myosin Vb as the molecular motor involved in movement towards the plasma membrane. We have also identified a family of at least 8 other Rab11 family interacting proteins (Rab11-FIPs) that also participate in the regulation of plasma membrane recycling. Present investigations center on understanding the assembly of endogenous complexes, the regulation of recycling by phosphorylation of Rab11-FIP proteins by the kinase Par1b/MARK2, and the influence of Rab11
The Goldenring laboratory studies a number of subjects that apply broadly to epithelial biology. We pursue three distinct programmatic areas. First, we are investigating the protein machinery required for the regulation of the recycling to the plasma membrane of receptors, ion transporters and ion channels. These studies focus on the ability of the Rab11 family of small GTPases (Rab11a, Rab11b and Rab25) to initiate and coordinate the assembly of multiprotein complexes regulating vesicle trafficking. Over the past several years, we have identified myosin Vb as the molecular motor involved in movement towards the plasma membrane. We have also identified a family of at least 8 other Rab11 family interacting proteins (Rab11-FIPs) that also participate in the regulation of plasma membrane recycling. Present investigations center on understanding the assembly of endogenous complexes, the regulation of recycling by phosphorylation of Rab11-FIP proteins by the kinase Par1b/MARK2, and the influence of Rab11
C2 domain second repeat present in Synaptotagmin-like proteins 1-4. All Slp members basically share an N-terminal Slp homology domain (SHD) and C-terminal tandem C2 domains (named the C2A domain and the C2B domain) with the SHD and C2 domains being separated by a linker sequence of various length. Slp1/JFC1 and Slp2/exophilin 4 promote granule docking to the plasma membrane. Additionally, their C2A domains are both Ca2+ independent, unlike the case in Slp3 and Slp4/granuphilin in which their C2A domains are Ca2+ dependent. It is thought that SHD (except for the Slp4-SHD) functions as a specific Rab27A/B-binding domain. In addition to Slps, rabphilin, Noc2, and Munc13-4 also function as Rab27-binding proteins. It has been demonstrated that Slp3 and Slp4/granuphilin promote dense-core vesicle exocytosis. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta ...
The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. That Rab regulates endocytic recycling. Acts as a major regulator of membrane delivery during cytokinesis. Together with MYO5B and RAB8A participates in epithelial cell polarization. Together with RAB3IP, RAB8A, the exocyst complex, PARD3, PRKCI, ANXA2, CDC42 and DNMBP promotes transcytosis of PODXL to the apical membrane initiation sites (AMIS), apical surface formation and lumenogenesis. Together with MYO5B participates in CFTR trafficking to the plasma membrane and TF (Transferrin) recycling in nonpolarized cells. Required in a complex with MYO5B and RAB11FIP2 for the transport of NPC1L1 to the plasma membrane. Participates in
Probable catalytic subunit of a GTPase activating protein that has specificity for Rab3 subfamily (RAB3A, RAB3B, RAB3C and RAB3D). Rab3 proteins are involved in regulated exocytosis of neurotransmitters and hormones. Specifically converts active Rab3-GTP to the inactive form Rab3-GDP. Required for normal eye and brain development. May participate in neurodevelopmental processes such as proliferation, migration and differentiation before synapse formation, and non-synaptic vesicular release of neurotransmitters.
Epithelial cells maintain intercellular communication directly by cell-cell, cell-ECM interaction and indirectly by paracrine secretion of extracellular messengers either as free molecules or via exosomes. The vesicular trafficking machinery is an integral part of such communication, paralleling digital cables that transmit the information bytes to the correct hub. During the process of EMT, derailing of the trafficking machinery leads to a systemic breakdown of intra and inter-cellular communication pathways. The purpose of the current study is to elucidate the functional role of Rab25, a key member of the vesicular trafficking machinery in mediating EMT-MET processes during breast cancer progression.. Aberrant endocytosis is a new hallmark of cancer. Rab GTPases are the primary regulators of endocytosis. Many members of this large family are implicated in a wide array of cancers including breast cancer. Specifically, Rab25, a GTPase associated with the recycling endosomes, is deregulated in ...
The tripartite DENN (after differentially expressed in neoplastic versus normal cells) domain is found in several proteins involved in Rab-mediated processes or regulation of MAPKs (Mitogen-activated preotein kinases) signaling pathways. It actually consists of three parts as the original DENN domain is always encircled on both sides by more divergent domains, called uDENN (after upstream DENN) and dDENN (for downstream DENN). The tripartite DENN domain is found associated with other domains, such as RUN, PLAT, PH, PPR, WD-40, GRAM or C1. The function of DENN domain remains to date unclear, although it appears to represent a good candidate for a GTP/GDP exchange activity [(PUBMED:11563850), (PUBMED:12906859)].. The general characteristics of DENN domains - three regions dDENN, DENN itself, and uDENN having different patterns of sequence conservation and separated by sequences of variable length - suggest that they are composed of at least three sub-domains which may feature distinct folds but ...
1. General Function. Rab1 is a small GTP binding protein that is expressed in virtually all mammalian cells, fish, worms and flies and is homologous to the yeast protein Ypt1 (3). It is essential for ER to Golgi transport and has also been implicated in intra Golgi transport (22, 30). There are two isoforms Rab1a (205 aa) and Rab1b (201aa) which are 92% identical at the amino acid level with most differences in the carboxyl terminus (28). These two isoforms are generally localized in the same cellular regions and have similar biochemical properties and functions. Rab1a may also play a role in transcytosis (14). In addition to localization by immunoflourescence in tissue culture cells, Rab1a has been localized by immunogold labeling to vesicles between the ER and Golgi region and over Golgi stacks in NRK cells (23).. The vesicular transport activity of Rab1 is dependent on its GTPase activity as a GDP bound mutant form, Rab1aS25N and the nucleotide free mutant (N124I) block transport from ER to ...
GCC185, a trans-Golgi network-localized protein predicted to assume a long, coiled-coil structure, is required for Rab9-dependent recycling of mannose 6-phosphate receptors (MPRs) to the Golgi and for microtubule nucleation at the Golgi via CLASP proteins. GCC185 localizes to the Golgi by cooperative interaction with Rab6 and Arl1 GTPases at adjacent sites near its C terminus. We show here by yeast two-hybrid and direct biochemical tests that GCC185 contains at least four additional binding sites for as many as 14 different Rab GTPases across its entire length. A central coiled-coil domain contains a specific Rab9 binding site, and functional assays indicate that this domain is important for MPR recycling to the Golgi complex. N-Terminal coiled-coils are also required for GCC185 function as determined by plasmid rescue after GCC185 depletion by using small interfering RNA in cultured cells. Golgi-Rab binding sites may permit GCC185 to contribute to stacking and lateral interactions of Golgi cisternae as
Background Ypt/Rab GTPases and their GEF activators regulate intra-cellular trafficking in every eukaryotic cells. Furthermore, the primary, aswell as the forecasted secondary, structure from the Trs120- and Trs130-related sequences are conserved from fungi to pets. The mammalian orthologs of Trs130 and Trs120, TMEM1 and NIBP, respectively, are applicants for individual disorders. Presently, NIBP is normally implicated in signaling, and TMEM1 is normally suggested to possess trans-membrane domains (TMDs) also to work as a membrane route. However, we present here which the yeast Trs130 will not work as a trans-membrane proteins, and the individual TMEM1 will not contain putative TMDs. The nonessential subunit, Trs65, is normally conserved just among many fungi plus some unicellular eukaryotes. Multiple position analysis of every TRAPPII-specific subunit uncovered conserved domains including highly conserved proteins. Conclusion We claim that the function of both NIBP and TMEM1 in the legislation ...
Subcellular distribution of wild-type and mutant Rab24 expressed in 293 cells. (A) Cells were transfected with vectors encoding mycRab24wt or mycRab24(D123I) an
Strict spatiotemporal control of trafficking events between organelles is critical for maintaining homeostasis and directing cellular responses. This regulation is particularly important in immune cells for mounting specialized immune defences. By controlling the formation, transport and fusion of intracellular organelles, Rab GTPases serve as master regulators of membrane trafficking. In this review, we discuss the cellular and molecular mechanisms by which Rab GTPases regulate immunity and inflammation.
TY - JOUR. T1 - Rab1 interacts directly with the β2-adrenergic receptor to regulate receptor anterograde trafficking. AU - Hammad, Maha. AU - Kuang, Yi Qun. AU - Morse, Alexa. AU - Dupré, Denis J.. PY - 2012/5/1. Y1 - 2012/5/1. N2 - Very little is understood about the trafficking of G protein-coupled receptors (GPCRs) from the endoplasmic reticulum (ER) to the plasma membrane. Rab guanosine triphosphatases (GTPases) are known to participate in the trafficking of various GPCRs via a direct interaction during the endocytic pathway, but whether this occurs in the anterograde pathway is unknown. We evaluated the potential interaction of Rab1, a GTPase known to regulate β2-adrenergic receptor (β2AR) trafficking, and its effect on export from the ER. Our results show that GTP-bound Rab1 interacts with the F(x) 6LL motif of β2AR. Receptors lacking the interaction motif fail to traffic properly, suggesting that a direct interaction with Rab1 is required for β2AR anterograde trafficking.. AB - Very ...
... Rab35 Activation Assay Kit bases on the configuration-specific anti-Rab35-GTP monoclonal antibody to measure the active Rab35-GTP levels, either from cell extracts or from in vitro GTPγS loading Rab35 activation assays. Briefly, anti-active Rab35 mouse monoclonal antibody will be incubated with cell lysates containing Rab35-GTP. The bound active Rab35 will then be pulled down by protein A/G agarose. The precipitated active Rab35 will be detected by immunoblot analysis using anti- Rab35 rabbit polyclonal antibody. ...
... Rab7 Activation Assay Kit bases on the configuration-specific anti-Rab7-GTP monoclonal antibody to measure the active Rab7-GTP levels, either from cell extracts or from in vitro GTPγS loading Rab7 activation assays. Briefly, anti-active Rab7 mouse monoclonal antibody will be incubated with cell lysates containing Rab7-GTP. The bound active Rab7 will then be pulled down by protein A/G agarose. The precipitated active Rab7 will be detected by immunoblot analysis using anti- Rab7 rabbit polyclonal antibody. ...
Reactome is pathway database which provides intuitive bioinformatics tools for the visualisation, interpretation and analysis of pathway knowledge.
Gao, X. D.; Albert, S.; Tcheperegine, S. E.; Burd, C. G.; Gallwitz, D.; Bi, E.: The GAP activity of Msb3p and Msb4p for the Rab GTPase Sec4p is required for efficient exocytosis and actin organization. Journal of Cell Biology 162 (4), pp. 635 - 646 (2003 ...
The neuronal protein GRASP-1 is shown to be a key molecule controlling endosomal trafficking and thereby regulating synapse integrity and synaptic plasticity.
Buy our Recombinant Human Rab5b protein. Ab104545 is a full length protein produced in Escherichia coli and has been validated in SDS-PAGE, MS. Abcam provides…
Buy our Recombinant Human Rab4 protein. Ab109957 is a full length protein produced in Escherichia coli and has been validated in SDS-PAGE, MS. Abcam provides…
Using probabilistic models and advanced tree building methods, we have been able to build the most comprehensive evolutionary tree of the Rab family that has been reported to date. In our analysis, we defined the Rab family as being distinct from the Ran family, and thus excluded some proteins which have been referred to as Rab-like but which are more likely to be Ran-like or have roles distinct from Rabs. These include RabL2, RabL3, and RabL5.. Our findings confirm and extend the evidence that the LECA had a large number of Rabs [16]. If our size estimate of LECA Rab repertoire is incorrect, it will, if anything, prove to be an underestimate once more genome sequences become available from non-metazoan organisms, in particular protozoa. Indeed after our analysis was completed, Elias et al. [60] reported an analysis of LECA Rabs using a different method to identify evolutionary relationships applied to only 55 species, and concluded that the LECA could have contained 23 Rabs. Although this ...
RAB3IL1 - RAB3IL1 (untagged)-Human RAB3A interacting protein (rabin3)-like 1 (RAB3IL1) available for purchase from OriGene - Your Gene Company.
Complete information for RAB32 gene (Protein Coding), RAB32, Member RAS Oncogene Family, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
Compare rabaptin, RAB GTPase binding effector protein 2 ELISA Kits from leading suppliers on Biocompare. View specifications, prices, citations, reviews, and more.
Rab6b - Rab6b (untagged) - Mouse RAB6B, member RAS oncogene family (Rab6b), (10ug) available for purchase from OriGene - Your Gene Company.
Complete information for RAB42 gene (Protein Coding), RAB42, Member RAS Oncogene Family, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
☎ Buy iStorage datAshur IS-FL-DA-256-8 8GB USB2 Key (Aluminium) - 256-bit FIPS at the best price » Same / Next Day Delivery WorldWide -- ✔ FREE Business Quotes ☎Call for pricing +44 20 8288 8555 [email protected] ✓Free Advice
The protein encoded by this gene belongs to the synaptotagmin-like (Slp) protein family, which contains a unique homology domain at the N-terminus, referred to as the Slp homology domain (SHD). The SHD functions as a binding site for Rab27A, which plays a role in protein transport. Expression of this gene is restricted to placenta and liver, suggesting that it might be involved in Rab27A-dependent membrane trafficking in specific tissues. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Sep 2009] ...
Mouse polyclonal antibody raised against a full-length human RAB9B protein. RAB9B (NP_057454.1, 1 a.a. ~ 201 a.a) full-length human protein. (H00051209-B01P) - Products - Abnova
Mouse polyclonal antibody raised against a full-length human RAB32 protein. RAB32 (NP_006825, 1 a.a. ~ 225 a.a) full-length human protein. (H00010981-B02P) - Products - Abnova
Protein syn cael ei godio yn y corff dynol gan y genyn RAB6B yw RAB6B a elwir hefyd yn Ras-related protein Rab-6B a RAB6B, member RAS oncogene family (Saesneg). Segment o DNA ywr genyn, syn amgodio ffwythiant arbennig. Maer genyn yma wedi ei leoli ar yr edefyn ôl o gromosom dynol 3, band 3q22.1.[2] ...
RAB7A antibody [Rab7-117] (RAB7A, member RAS oncogene family) for ELISA, ICC/IF, IP, WB. Anti-RAB7A mAb (GTX16196) is tested in Human, Mouse, Chicken, Monkey, Rat, Bovine samples. 100% Ab-Assurance.