• 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)
  • 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)
  • 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 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)
  • 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)
  • 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)
  • 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)
  • 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)
  • 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)
  • 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)
  • The fission yeast Schizosaccharomyces japonicus provides an attractive stripped-down model for metabolic compartmentalization in peroxisomes. (biorxiv.org)
  • The actin protein is found in both the cytoplasm and the cell nucleus. (wikipedia.org)
  • Mediates importin-alpha re-export from the nucleus to the cytoplasm after import substrates (cargos) have been released into the nucleoplasm. (swisspalm.org)
  • functional characterization of nat/ncs2 proteins of aspergillus brasiliensis reveals a genuine xanthine-uric acid transporter and an intrinsically misfolded polypeptide. (liverpool.ac.uk)
  • A hydrophobic amino acid, most frequently leucine although all amino acids with hydrophobic side chains (except tyrosine) are allowed (alanine, valine, isoleucine, leucine, methionine, phenylalanine and trypthophan) is the first position. (eu.org)
  • This is followed most frequently by a stretch of four positions where every amino acid is allowed, although there are occurrences where the hydrophobic amino acid shifted one position upstream or downstream. (eu.org)
  • After a stretch of 3 to 6 flexible positions where every amino acid is allowed (frequently, at least one of these positions is serine), a negatively charged sequence of at least 3 aspartic acids and/or glutamic acids follows. (eu.org)
  • Actin is a family of globular multi-functional proteins that form microfilaments in the cytoskeleton, and the thin filaments in muscle fibrils. (wikipedia.org)
  • An actin protein is the monomeric subunit of two types of filaments in cells: microfilaments, one of the three major components of the cytoskeleton, and thin filaments, part of the contractile apparatus in muscle cells. (wikipedia.org)
  • 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)
  • Third, actin filaments can bind to many other proteins, which together help modify and organize microfilaments for their diverse functions. (wikipedia.org)
  • This work aimed to clarify the solubilization mechanism by deciphering myosin thick filaments assembly as affected by protein-glutaminase deamidation. (bvsalud.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 large number of illnesses and diseases are caused by mutations in alleles of the genes that regulate the production of actin or of its associated proteins. (wikipedia.org)
  • As peroxisomes grow and mature, cargo import into the peroxisomal matrix takes place. (biorxiv.org)
  • The ER is the 'port of entry' for proteins destined for the cell surface and beyond. (stanford.edu)
  • Instead, damaged or incorrectly synthesized proteins must be rapidly and efficiently destroyed lest they form toxic aggregates. (stanford.edu)
  • Actin is extremely abundant in most cells, comprising 1-5% of the total protein mass of most cells, and 10% of muscle cells. (wikipedia.org)
  • Enzymatic deamidation is a promising approach in enhancing the solubility of myofibrillar proteins (MPs) in water paving the way of tailor manufacturing muscle protein-based beverages. (bvsalud.org)
  • A beta-hairpin comprising the nuclear localization sequence sustains the self-associated states of nucleosome assembly protein 1. (colorado.edu)
  • However, domains required for cargo transport in vivo have not been mapped. (go.jp)
  • Actin is a family of globular multi-functional proteins that form microfilaments in the cytoskeleton, and the thin filaments in muscle fibrils. (wikipedia.org)
  • An actin protein is the monomeric subunit of two types of filaments in cells: microfilaments, one of the three major components of the cytoskeleton, and thin filaments, part of the contractile apparatus in muscle cells. (wikipedia.org)
  • The evolutionary origin of actin can be traced to prokaryotic cells, which have equivalent proteins. (wikipedia.org)
  • A large number of illnesses and diseases are caused by mutations in alleles of the genes that regulate the production of actin or of its associated proteins. (wikipedia.org)
  • Third, actin filaments can bind to many other proteins, which together help modify and organize microfilaments for their diverse functions. (wikipedia.org)
  • Actin is extremely abundant in most cells, comprising 1-5% of the total protein mass of most cells, and 10% of muscle cells. (wikipedia.org)
  • The actin protein is found in both the cytoplasm and the cell nucleus. (wikipedia.org)
  • Proteome profiling and global protein-interaction approaches have significantly improved our knowledge of the protein interactomes of autophagy and other cellular stress-response pathways. (nih.gov)
  • Here, using fluorescence microscopy and cell lines expressing endogenously tagged proteins, we mapped the subcellular localization of 89% of the T. brucei proteome, a resource we call TrypTag. (nature.com)
  • New discoveries regarding protein complexes, interaction partners, interaction domains, and biological roles of players that are part of these pathways are emerging. (nih.gov)
  • The major protein import pathways, including the presequence pathway (TIM23 pathway), the carrier pathway (TIM22 pathway), and the mitochondrial intermembrane space import and assembly machinery, related translocases, proteinases, and chaperones, are discussed here. (biomed.news)
  • Ascribing subcellular localization of proteins assists understanding function and has largely been addressed through 'omic' approaches, such as proteomics of purified organelles and hyperplexed organelle localizations by isotope tagging 1 . (nature.com)
  • Mitochondrial protein import systems function not only as independent units for protein translocation, but also are deeply integrated into a functional network of mitochondrial bioenergetics, protein quality control, mitochondrial dynamics and morphology, and interaction with other organelles. (biomed.news)
  • Mitochondrial protein import deficiency is linked to various diseases, including cardiovascular disease. (biomed.news)
  • Protein localization offers insights into organelle subdomains/dynamics and cell-cycle-dependent localization changes. (nature.com)
  • Manual 26.29 HN - 2002 MH - Activin Receptors UI - D029404 MN - D8.586.913.696.620.682.700.62 MN - D12.776.543.750.750.400.820.500 MS - Receptors for ACTIVINS are membrane protein kinases belonging to the family of PROTEIN-SERINE-THREONINE KINASES, thus also named activin receptor-like kinases (ALK's). (nih.gov)
  • 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)