Many viruses use the microtubule transport system to transport nucleic acid/protein cores to intracellular replication sites after invasion host the cell membrane. (wikipedia.org)
The recruitment of specific cytosolic proteins to intracellular membranes through binding phosphorylated derivatives of phosphatidylinositol (PtdIns) controls such processes as endocytosis, regulated exocytosis, cytoskeletal organization, and cell signaling. (embl.de)
Biosynthesis and intracellular targeting of the CLN3 protein defective in Batten disease. (ac.ir)
Success will represent an unprecedented level of control over nanoscale motion, building an engineering capacity that will eventually be used to design protein nanoassemblies capable of sophisticated intracellular therapeutic functions such as genome repair. (nih.gov)
Homologous1
the filamentous fungus aspergillus oryzae is a well-known expression host used to express homologous and heterologous proteins in a number of industrial applications. (liverpool.ac.uk)
Motor proteins2
Dyneins are a family of cytoskeletal motor proteins that move along microtubules in cells. (wikipedia.org)
In contrast, most kinesin motor proteins move toward the microtubules' plus-end, in what is called anterograde transport. (wikipedia.org)
Membrane4
Protein modules such as FVYE domains and PH domains that bind specifically to PtdIns 3-phosphate (PtdIns-3-P) and polyphosphoinositides, respectively, can direct such membrane targeting. (embl.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)
VCP complexes are involved in many cellular processes, particularly in the endoplasmic reticulum (ER)‐associated degradation (ERAD) process for protein quality control, membrane trafficking, and DNA damage response. (eu.org)
ERAD enables ER processing to distinguish the properly and improperly folded proteins in the ER lumen and then extracts them through membrane channels (dislocation or retrotranslocation) in an energy-dependent manner for delivery to cytosolic proteasomes. (eu.org)
For instance, how can cells control the diverse patterns of glycosylation of various secretory proteins in the endoplasmic reticulum and Golgi in an orderly manner with high accuracy? (go.jp)
The Endoplasmic Reticulum (ER) is an important eukaryotic cell organelle that has various functions, including the synthesis of proteins for export and quality control of nascent proteins. (eu.org)
Nuclear3
Nuclear mRNA transcripts acquire a protein coat composed of cap- and RNA-binding proteins that allow nuclear export and dictate the functional program of cytoplasmic mRNAs ( Moore, 2005 ). (rupress.org)
We found that the FERM domain in the tail region, which is known to bind to lipids as well as other proteins, is essential for both nuclear and chloroplast positioning, whereas the proximal MyTH4 domain plays a supporting role in chloroplast transport. (go.jp)
A beta-hairpin comprising the nuclear localization sequence sustains the self-associated states of nucleosome assembly protein 1. (colorado.edu)
Cytoplasmic2
The force-generating ATPase activity of each dynein heavy chain is located in its large doughnut-shaped "head", which is related to other AAA proteins, while two projections from the head connect it to other cytoplasmic structures. (wikipedia.org)
The C-terminal tail of ribosomal protein Rps15 is engaged in cytoplasmic pre-40S maturation. (db-engine.de)
Lumen1
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)
Secretory3
The PI3K/Akt/mTOR signaling pathway is a key regulator of diverse physiological functions such as proliferation, global protein, and lipid synthesis as well as many metabolic pathways interacting to increase secretory capabilities. (go.jp)
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)
Our goal is to elucidate the functional networks that coordinate protein synthesis and quality control in the early secretory pathway. (stanford.edu)
Mitosis2
Dynein transports various cellular cargos, provides forces and displacements important in mitosis, and drives the beat of eukaryotic cilia and flagella. (wikipedia.org)
While a postdoctoral student at MIT, Tomomi Kiyomitsu discovered how dynein has a role as a motor protein in aligning the chromosomes in the middle of the cell during the metaphase of mitosis. (wikipedia.org)
Biosynthesis1
Here we probe these fundamental questions using peroxisomal compartmentalization of the last steps of lysine and histidine biosynthesis in the fission yeast Schizosaccharomyces japonicus . (biorxiv.org)
Lysine1
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)
Yeast4
The fission yeast Schizosaccharomyces japonicus provides an attractive stripped-down model for metabolic compartmentalization in peroxisomes. (biorxiv.org)
Members of a subfamily of these enzymes share a specific domain that was first identified in the yeast Sac1 protein [1]. (embl.de)
Despite the detailed in vitro characterization of the enzymatic properties of yeast Sac1p, the exact cellular function of this protein has remained obscure. (embl.de)
Ter94 in fly, CDC48 in yeast) is a hexameric multidomain protein belonging to the functionally highly diverse AAA+ (ATPases Associated with diverse cellular Activities) superfamily of proteins. (eu.org)
Cellular1
VCP (P97, TERA) is an essential and abundant AAA-ATPase that mediates vital cellular activities with the cooperation of many cofactors. (eu.org)
Functional1
functional characterization of nat/ncs2 proteins of aspergillus brasiliensis reveals a genuine xanthine-uric acid transporter and an intrinsically misfolded polypeptide. (liverpool.ac.uk)
Mechanisms2
Different classes of RNA granules share some protein components and may use similar mechanisms to regulate mRNA translation/decay. (rupress.org)
A next step in studying the complex interaction between host and microbe is to "directly" define the molecular factors that govern biological function (i.e. proteins, metabolites, posttranslational modifications) and delineate their associated mechanisms of action. (keystonesymposia.org)
Post-translational2
At its core, the laboratory develops and applies multiplexing quantitative proteomics tools to simultaneously track thousands of protein dynamics and associated post-translational modifications in an accurate and high throughput fashion. (keystonesymposia.org)
Newly synthesized proteins undergo folding and post-translational modifications in the ER. (eu.org)
Lipid1
Phosphoinositide phosphatases play an essential but as yet not well-understood role in lipid-based signal transduction. (embl.de)
Dynein2
Each molecule of the dynein motor is a complex protein assembly composed of many smaller polypeptide subunits. (wikipedia.org)
The other projection, the extended tail, binds to the light intermediate, intermediate and light chain subunits which attach dynein to its cargo. (wikipedia.org)
Complexes1
Transformation of Chaetomium thermophilum and affinity-purification of native thermostable protein complexes. (db-engine.de)
Mechanism2
This work aimed to clarify the solubilization mechanism by deciphering myosin thick filaments assembly as affected by protein-glutaminase deamidation. (bvsalud.org)
The ERAD (ER-Associated Degradation) mechanism acts as a protein quality control and removes these misfolded proteins. (eu.org)
Function1
Juvenile neuronal ceroid lipofuscinosis (JNCL), one of the most frequent forms of the NCL storage diseases, is known to be caused by loss-of-function mutations in ceroid-lipofuscinosis neuronal protein 3 (CLN3), but its cell function has not been fully elucidated. (ac.ir)
Complex2
Structural inventory of cotranslational protein folding by the eukaryotic RAC complex, Structural inventory of cotranslational protein folding by the eukaryotic RAC complex, Nat. (db-engine.de)
N-SLIT2 amplifies reactive oxygen species production in response to the bacteria by activating p38 mitogen-activated protein kinase that in turn phosphorylates NCF1, an essential subunit of the NADPH oxidase complex. (elifesciences.org)
Chains1
Nearly all ERAD substrates are ubiquitinated prior to their degradation and these ubiquitin chains provide a binding site for VCP (Valosin-Containing Protein). (eu.org)
Made1
Unlike DNA, which can be repaired if damaged or incorrectly made, proteins cannot be mended. (stanford.edu)
Process1
Some mRNAs are programmed for immediate translation, a process that remodels the protein coat and assembles a polysome. (rupress.org)
Group1
The N-terminal domain of VCP acts as a binding site for a group of adaptor proteins through their Arg/Lys-rich peptide motifs. (eu.org)
Import1
As peroxisomes grow and mature, cargo import into the peroxisomal matrix takes place. (biorxiv.org)
Evolution1
Though the VCP and their binding partners are conserved in eukaryotes, the sequences that mediate their interactions are significantly different across organisms showing that evolution has established more than one way for these proteins to interact. (eu.org)
Role1
Thus, GCGs contain proteins involved in translation initiation, translation control, and mRNA decay, which is consistent with their proposed role in the regulation ofs maternal mRNA expression. (rupress.org)