Molecular chaperones and intracellular protein translocation

2006 ◽  
pp. 199-264 ◽  
Author(s):  
Joachim Rassow ◽  
Nikolaus Pfanner
Keyword(s):  
Molecular Chaperones ◽  
Protein Translocation ◽  
Intracellular Protein

scholarly journals Imaging the dynamics of intracellular protein translocation by photoconversion of phamret-cybr/ROM

2010 ◽  
Vol 242 (3) ◽  
pp. 250-261
Author(s):  
L. YANG ◽  
T. MATSUDA ◽  
V. RAVIRAJ ◽  
Y. W. CHING ◽  
F. BRAET ◽  
...  
Keyword(s):  
Protein Translocation ◽  
Intracellular Protein

scholarly journals Mitochondrial molecular chaperones: their role in protein translocation

1994 ◽  
Vol 19 (2) ◽  
pp. 87-92 ◽  
Author(s):  
Rosemary A. Stuart ◽  
Douglas M. Cyr ◽  
Elizabeth A. Craig ◽  
Walter Neupert
Keyword(s):  
Molecular Chaperones ◽  
Protein Translocation

The role of molecular chaperones in protein transport into the endoplasmic reticulum

1993 ◽  
Vol 339 (1289) ◽  
pp. 335-341 ◽  
Keyword(s):  
Endoplasmic Reticulum ◽  
Molecular Chaperones ◽  
Protein Transport ◽  
Protein Translocation ◽  
Signal Recognition Particle ◽  
Microsomal Membrane ◽  
Nucleoside Triphosphate ◽  
Secretory Proteins ◽  
Hsc 70 ◽  
Hydrolysis Of

In eukaryotic cells export of the vast majority of newly synthesized secretory proteins is initiated at the level of the membrane of the endoplasmic reticulum (microsomal membrane). The precursors of secretory proteins are not transported across the microsomal m em brane in their native state. Typically, signal peptides in the precursor proteins are involved in preserving the transport-competent state. Furthermore, there are two alternatively acting mechanisms involved in preserving transport competence in the cytosol. The first mechanism involves two ribonucleoparticles (ribosome and signal recognition particle) and their receptors on the microsomal surface and requires the hydrolysis of GTP. The second mechanism does not involve ribonucleoparticles and their receptors but depends on the hydrolysis of A TP and on cA-acting molecular chaperones, such as heat shock cognate protein 70 (hsc 70). In both mechanisms a translocase in the microsomal membrane mediates protein translocation. This translocase includes a signal peptide receptor on the cu-side of the microsomal membrane and a component that also depends on the hydrolysis of ATP. At least in certain cases, an additional nucleoside triphosphate-requiring step is involved which is related to the trans -acting molecular chaperone BiP.

Cellular strategies to cope with protein aggregation

2016 ◽  
Vol 60 (2) ◽  
pp. 153-161 ◽  
Author(s):  
Annika Scior ◽  
Katrin Juenemann ◽  
Janine Kirstein
Keyword(s):  
Protein Aggregation ◽  
Molecular Chaperones ◽  
Protein Aggregates ◽  
Misfolded Proteins ◽  
Protein Species ◽  
Intracellular Protein ◽  
Controlled Deposition ◽  
Control Protein

Nature has evolved several mechanisms to detoxify intracellular protein aggregates that arise upon proteotoxic challenges. These include the controlled deposition of misfolded proteins at distinct cellular sites, the protein disaggregation and refolding by molecular chaperones and/or degradation of misfolded and aggregated protein species by cellular clearance pathways. In this article, we discuss cellular the strategies of prokaroytes and eukaryotes to control protein aggregation.

scholarly journals Regulation of Annexin I in Rheumatoid Synovial Cells by Glucocorticoids and Interleukin-1

2006 ◽  
Vol 2006 ◽  
pp. 1-6 ◽  
Author(s):  
Eric F. Morand ◽  
Pam Hall ◽  
Paul Hutchinson ◽  
Yuan H. Yang
Keyword(s):  
Rheumatoid Arthritis ◽  
Protein Translocation ◽  
Interleukin 1 ◽  
Signalling Pathways ◽  
Synovial Cells ◽  
Additive Effects ◽  
Intracellular Protein ◽  
Annexin I ◽  
Antiinflammatory Effects ◽  
Fibroblast Like Synoviocytes

The glucocorticoid (GC)-induced antiinflammatory molecule annexin I is expressed in leukocytes and has antiinflammatory effects in animal models of arthritis, but the expression of annexin I in rheumatoid arthritis (RA) fibroblast-like synoviocytes (FLS) is unknown. We report the constitutive and dexamethasone (DEX)-inducible expression of annexin I in RA FLS. DEX increased FLS annexin I protein translocation and mRNA expression. Interleukin (IL)-1βalso induced annexin I translocation and mRNA but also increased intracellular protein. DEX and IL-1 had additive effects on annexin I mRNA, but DEX inhibited the inducing effect of IL-1βon cell surface annexin I. These results indicate that glucocorticoids and IL-1βupregulate the synthesis and translocation of annexin I in RA FLS, but interdependent signalling pathways are involved.

Androgen-induced plasticity at a “vocal” neuromuscular synapse

1994 ◽  
Vol 52 ◽  
pp. 32-33
Author(s):  
Darcy B. Kelley ◽  
Martha L. Tobias ◽  
Mark Ellisman
Keyword(s):  
Xenopus Laevis ◽  
Motor Neurons ◽  
Sexual Differentiation ◽  
Molecular Basis ◽  
Neuromuscular Synapse ◽  
Sexually Dimorphic ◽  
Intracellular Protein ◽  
Developmental Program ◽  
Androgen Action ◽  
Clawed Frog

Brain and muscle are sexually differentiated tissues in which masculinization is controlled by the secretion of androgens from the testes. Sensitivity to androgen is conferred by the expression of an intracellular protein, the androgen receptor. A central problem of sexual differentiation is thus to understand the cellular and molecular basis of androgen action. We do not understand how hormone occupancy of a receptor translates into an alteration in the developmental program of the target cell. Our studies on sexual differentiation of brain and muscle in Xenopus laevis are designed to explore the molecular basis of androgen induced sexual differentiation by examining how this hormone controls the masculinization of brain and muscle targets.Our approach to this problem has focused on a highly androgen sensitive, sexually dimorphic neuromuscular system: laryngeal muscles and motor neurons of the clawed frog, Xenopus laevis. We have been studying sex differences at a synapse, the laryngeal neuromuscular junction, which mediates sexually dimorphic vocal behavior in Xenopus laevis frogs.

Spatial localization of unknown proteins in the endoplasmic reticulum predicts functions

2007 ◽  
Vol 30 (4) ◽  
pp. 84
Author(s):  
Michael D. Jain ◽  
Hisao Nagaya ◽  
Annalyn Gilchrist ◽  
Miroslaw Cygler ◽  
John J.M. Bergeron
Keyword(s):  
Endoplasmic Reticulum ◽  
Protein Folding ◽  
Protein Synthesis ◽  
Protein Function ◽  
Protein Translocation ◽  
Spatial Localization ◽  
Predict Protein Function ◽  
Insight Into ◽  
Soluble Fractions ◽  
Er Membrane

Protein synthesis, folding and degradation functions are spatially segregated in the endoplasmic reticulum (ER) with respect to the membrane and the ribosome (rough and smooth ER). Interrogation of a proteomics resource characterizing rough and smooth ER membranes subfractionated into cytosolic, membrane, and soluble fractions gives a spatial map of known proteins involved in ER function. The spatial localization of 224 identified unknown proteins in the ER is predicted to give insight into their function. Here we provide evidence that the proteomics resource accurately predicts the function of new proteins involved in protein synthesis (nudilin), protein translocation across the ER membrane (nicalin), co-translational protein folding (stexin), and distal protein folding in the lumen of the ER (erlin-1, TMX2). Proteomics provides the spatial localization of proteins and can be used to accurately predict protein function.

Sign in / Sign up

Export Citation Format

Share Document