Literature DB >> 21291501

Molecular mechanism of co-translational protein targeting by the signal recognition particle.

Ishu Saraogi1, Shu-ou Shan.   

Abstract

The signal recognition particle (SRP) is a key component of the cellular machinery that couples the ongoing synthesis of proteins to their proper localization, and has often served as a paradigm for understanding the molecular basis of protein localization within the cell. The SRP pathway exemplifies several key molecular events required for protein targeting to cellular membranes: the specific recognition of signal sequences on cargo proteins, the efficient delivery of cargo to the target membrane, the productive unloading of cargo to the translocation machinery and the precise spatial and temporal coordination of these molecular events. Here we highlight recent advances in our understanding of the molecular mechanisms underlying this pathway, and discuss new questions raised by these findings.
© 2011 John Wiley & Sons A/S.

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Year:  2011        PMID: 21291501      PMCID: PMC3077218          DOI: 10.1111/j.1600-0854.2011.01171.x

Source DB:  PubMed          Journal:  Traffic        ISSN: 1398-9219            Impact factor:   6.215


  64 in total

Review 1.  Signal sequences.

Authors:  L M Gierasch
Journal:  Biochemistry       Date:  1989-02-07       Impact factor: 3.162

Review 2.  Signal sequences: the same yet different.

Authors:  N Zheng; L M Gierasch
Journal:  Cell       Date:  1996-09-20       Impact factor: 41.582

3.  Both lumenal and cytosolic gating of the aqueous ER translocon pore are regulated from inside the ribosome during membrane protein integration.

Authors:  S Liao; J Lin; H Do; A E Johnson
Journal:  Cell       Date:  1997-07-11       Impact factor: 41.582

Review 4.  Signal sequence recognition and protein targeting to the endoplasmic reticulum membrane.

Authors:  P Walter; A E Johnson
Journal:  Annu Rev Cell Biol       Date:  1994

5.  Signal sequences. The limits of variation.

Authors:  G von Heijne
Journal:  J Mol Biol       Date:  1985-07-05       Impact factor: 5.469

6.  Model for signal sequence recognition from amino-acid sequence of 54K subunit of signal recognition particle.

Authors:  H D Bernstein; M A Poritz; K Strub; P J Hoben; S Brenner; P Walter
Journal:  Nature       Date:  1989-08-10       Impact factor: 49.962

7.  SRP samples nascent chains for the presence of signal sequences by interacting with ribosomes at a discrete step during translation elongation.

Authors:  S C Ogg; P Walter
Journal:  Cell       Date:  1995-06-30       Impact factor: 41.582

8.  Each of the activities of signal recognition particle (SRP) is contained within a distinct domain: analysis of biochemical mutants of SRP.

Authors:  V Siegel; P Walter
Journal:  Cell       Date:  1988-01-15       Impact factor: 41.582

9.  The affinity of signal recognition particle for presecretory proteins is dependent on nascent chain length.

Authors:  V Siegel; P Walter
Journal:  EMBO J       Date:  1988-06       Impact factor: 11.598

10.  The signal recognition particle receptor is a complex that contains two distinct polypeptide chains.

Authors:  S Tajima; L Lauffer; V L Rath; P Walter
Journal:  J Cell Biol       Date:  1986-10       Impact factor: 10.539

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  41 in total

Review 1.  The delicate balance between secreted protein folding and endoplasmic reticulum-associated degradation in human physiology.

Authors:  Christopher J Guerriero; Jeffrey L Brodsky
Journal:  Physiol Rev       Date:  2012-04       Impact factor: 37.312

2.  Large-scale analysis of conserved rare codon clusters suggests an involvement in co-translational molecular recognition events.

Authors:  Matthieu Chartier; Francis Gaudreault; Rafael Najmanovich
Journal:  Bioinformatics       Date:  2012-03-30       Impact factor: 6.937

Review 3.  Protein secretion and the endoplasmic reticulum.

Authors:  Adam M Benham
Journal:  Cold Spring Harb Perspect Biol       Date:  2012-08-01       Impact factor: 10.005

4.  AtTPR7 as part of the Arabidopsis Sec post-translocon.

Authors:  Regina Schweiger; Serena Schwenkert
Journal:  Plant Signal Behav       Date:  2013-06-11

5.  YlxM is a newly identified accessory protein that influences the function of signal recognition particle pathway components in Streptococcus mutans.

Authors:  Matthew L Williams; Paula J Crowley; Adnan Hasona; L Jeannine Brady
Journal:  J Bacteriol       Date:  2014-03-21       Impact factor: 3.490

Review 6.  Protein folding and quality control in the ER.

Authors:  Kazutaka Araki; Kazuhiro Nagata
Journal:  Cold Spring Harb Perspect Biol       Date:  2011-11-01       Impact factor: 10.005

7.  Regulation by a chaperone improves substrate selectivity during cotranslational protein targeting.

Authors:  Aileen Ariosa; Jae Ho Lee; Shuai Wang; Ishu Saraogi; Shu-ou Shan
Journal:  Proc Natl Acad Sci U S A       Date:  2015-06-08       Impact factor: 11.205

8.  Evolution from the prokaryotic to the higher plant chloroplast signal recognition particle: the signal recognition particle RNA is conserved in plastids of a wide range of photosynthetic organisms.

Authors:  Chantal Träger; Magnus Alm Rosenblad; Dominik Ziehe; Christel Garcia-Petit; Lukas Schrader; Klaus Kock; Christine Vera Richter; Birgit Klinkert; Franz Narberhaus; Christian Herrmann; Eckhard Hofmann; Henrik Aronsson; Danja Schünemann
Journal:  Plant Cell       Date:  2012-12-28       Impact factor: 11.277

9.  Enhanced recombinant factor VII expression in Chinese hamster ovary cells by optimizing signal peptides and fed-batch medium.

Authors:  Lin Peng; Xiao Yu; Chengyuan Li; Yanfei Cai; Yun Chen; Yang He; Jianfeng Yang; Jian Jin; Huazhong Li
Journal:  Bioengineered       Date:  2016-04-26       Impact factor: 3.269

Review 10.  Potential Pathogenic Role of Anti-Signal Recognition Protein and Anti-3-hydroxy-3-methylglutaryl-CoA Reductase Antibodies in Immune-Mediated Necrotizing Myopathies.

Authors:  Leandro Ladislau; Louiza Arouche-Delaperche; Yves Allenbach; Olivier Benveniste
Journal:  Curr Rheumatol Rep       Date:  2018-08-03       Impact factor: 4.592

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