...-translational protein folding in the ER . Traffic 17 , 615 - 638 . 10.1111/tra.12392 Ellgaard , L. , Sevier , C. S. and Bulleid , N. J. ( 2018 ). How are proteins reduced in the endoplasmic reticulum? Trends Biochem. Sci. 43 , 32 - 43 . 10.1016/j.tibs.2017.10.006...

... how errors in membrane protein biogenesis can trigger co-translational degradation that employs machinery of the ribosome-associated quality control pathway. Endoplasmic reticulum Membrane protein Protein folding Ribosome Translation Medical Research Council 10.13039/501100007155...

... interests. © 2020. Published by The Company of Biologists Ltd 2020 Summary: A review of how ERp44 is key in sculpting the composition of the secretome and of the organelles of the early secretory pathway. ERp44 Protein folding Quality control Secretory pathway Zinc Fondazione...

... sensitivity demonstrates the requirement for a membrane protein to shuttle electrons from the cytosol to the ER. These results provide compelling evidence for the crucial role of the cytosol in regulating ER redox homeostasis, ensuring correct protein folding and facilitating the degradation of misfolded ER...

... responsibilities overseen by client proteins requiring the EMC for maturation. EMC Membrane protein Protein quality control Protein folding “la Caixa” Foundation 10.13039/100010434 The eukaryotic endoplasmic reticulum (ER) houses the machinery responsible for biogenesis of secreted...

... membrane, mediate protein folding and membrane protein topogenesis, and modify them chemically. In addition to co-translational protein import and translocation, distinct ER translocon complexes enable post-translational translocation and membrane integration. This post-translational pathway is widespread...

... 2015 Chaperone Protein folding Protein phosphatase 1 Cdc48 Shp1 Type 1 protein serine/threonine phosphatase (PP1) functions in many aspects of cell physiology in all eukaryotes ( Ceulemans and Bollen, 2004 ). PP1 consists of the catalytic subunit and various regulatory subunits...

... and in vitro assays, we show that proteins in the process of synthesis/folding are particularly sensitive to arsenite-induced aggregation, that arsenite interferes with protein folding by acting on unfolded polypeptides, and that arsenite directly inhibits chaperone activity. Thus, folding inhibition...

... a general strategy for both non-secretory and specialized secretory cells. * Present address: MRC Laboratory of Molecular Biology, Hills Road, Cambridge, CB2 0QH, UK ‡ Author for correspondence ( [email protected] ) 3 12 2009 © 2010. 2010 Protein folding Folding stress...

... Unconventional protein secretion Non-classical export Membrane translocation Fibroblast growth factor 2 FGF2 Protein folding Quality control The molecular mechanisms of unconventional secretory processes have been a long-standing mystery in molecular cell biology ( Muesch et al., 1990 ; Cleves...

... 11 12 2007 © The Company of Biologists Limited 2008 2008 HSP90 Molecular chaperones Protein folding Radicicol Heat shock protein 90 kDa (hereafter termed HSP90) works in an ATP-dependent manner to regulate the activity of a limited subset of medically relevant signalling...

... chaperones has revealed important new information on the mechanisms regulating protein folding and quality control. Tight regulation of N -glycan modifications is crucial to maintain protein quality control, to ensure the synthesis of functional polypeptides and to avoid constipation of the ER with folding...

... on the properties of skeletal-muscle actin. Biochem. J. 213 , 651 -659. Tokuriki, N., Kinjo, M., Negi, S., Hoshino, M., Goto, Y., Urabe, I. and Yomo, T. ( 2004 ). Protein folding by the effects of macromolecular crowding. Protein Sci. 13 , 125 -133. Uversky, V., Cooper, M., Bower, K., Li, J...

... that ERp57 participates in glycoprotein biogenesis either alone or in tandem with calnexin and calreticulin. e-mail: [email protected] 22 12 2005 © The Company of Biologists Limited 2006 2006 Calnexin Calreticulin Endoplasmic reticulum Quality control Protein folding...

... retention of SI Q1098P in ERGIC and cis-Golgi in phenotype II of CSID. * Author for correspondence (e-mail: [email protected] ) 9 3 2005 © The Company of Biologists Limited 2005 2005 Sucrase-isomaltase ER-quality control cis-Golgi ERGIC Protein folding...

...Zlatka Kostova; Dieter H. Wolf In the endoplasmic reticulum (ER), N -linked glycans (N-glycans) function as signals to recruit the lectin chaperones involved in protein folding, quality control and ER-associated degradation. We undertook a systematic study of the four N-glycans of mutated...

...Takunari Yoneda; Cristina Benedetti; Fumihiko Urano; Scott G. Clark; Heather P. Harding; David Ron Protein folding in the mitochondria is assisted by nuclear-encoded compartment-specific chaperones but regulation of the expression of their encoding genes is poorly understood. We found...

... 3QX, UK 23 2 2004 © The Company of Biologists Limited 2004 2004 Actin Nemaline myopathy Actin polymerization Protein folding Myopathy Actin mutations Congenital myopathies resulting from mutations in the gene encoding α-skeletal-muscle actin, ACTA1 , show various...

...Philippe Collin; Pascale B. Beauregard; Aram Elagöz; Luis A. Rokeach Calnexin is a molecular chaperone playing key roles in protein folding and the quality control of this process in the endoplasmic reticulum. We, and others, have previously demonstrated that cnx1 + , the gene encoding...

...-mail: [email protected] ) © The Company of Biologists Limited 2002 2002 UCS Myosin chaperone UNC-45 Protein folding Myosins are a large family of protein motors that contain at least 18 different classes. They interact with actin filaments to generate a broad spectrum of eukaryotic cell...