PMID- 22505607
OWN - NLM
STAT- MEDLINE
DCOM- 20130507
LR  - 20211021
IS  - 1477-9137 (Electronic)
IS  - 0021-9533 (Print)
IS  - 0021-9533 (Linking)
VI  - 125
IP  - Pt 15
DP  - 2012 Aug 1
TI  - TRC40 can deliver short secretory proteins to the Sec61 translocon.
PG  - 3612-20
AB  - Whilst the co-translational translocation of nascent proteins across the 
      mammalian endoplasmic reticulum (ER) is well defined, the capacity of this 
      organelle for post-translational translocation is poorly delineated. Here we 
      identify two human secretory protein precursors, apelin and statherin, as bona 
      fide substrates for post-translational translocation across the ER membrane. 
      Further studies, in combination with Hyalophora cecropia preprocecropin A 
      (ppcecA), show that all three proteins bind to TRC40 and can utilise this 
      component for their delivery to the ER membrane in a well-established in vitro 
      system. However, ppcecA is not an obligate TRC40 substrate, and it can also be 
      delivered to the ER by an alternative TRC40-independent pathway. Upon arrival at 
      the ER membrane, these short secretory proteins appear to be ubiquitously 
      transported across the ER membrane through the Sec61 translocon, apparently 
      irrespective of their delivery route. We speculate that the post-translational 
      translocation of secretory proteins in higher eukaryotes is more prevalent than 
      previously acknowledged.
FAU - Johnson, Nicholas
AU  - Johnson N
AD  - Faculty of Life Sciences, The University of Manchester, Michael Smith Building, 
      Oxford Road, Manchester M13 9PT, UK.
FAU - Vilardi, Fabio
AU  - Vilardi F
FAU - Lang, Sven
AU  - Lang S
FAU - Leznicki, Pawel
AU  - Leznicki P
FAU - Zimmermann, Richard
AU  - Zimmermann R
FAU - High, Stephen
AU  - High S
LA  - eng
GR  - BB/D005752/1/BB_/Biotechnology and Biological Sciences Research Council/United 
      Kingdom
GR  - WT092107/WT_/Wellcome Trust/United Kingdom
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20120414
PL  - England
TA  - J Cell Sci
JT  - Journal of cell science
JID - 0052457
RN  - 0 
      (1-(4-chlorophenyl)-3-(3-(4-chlorophenyl)-5,5-dimethyl-1-(3-(5-nitrofuran-2-yl)allyldienehydrazinocarbonylmethyl)-2-oxoimidazolidin-4-yl)-1-hydroxyurea)
RN  - 0 (APLN protein, human)
RN  - 0 (Apelin)
RN  - 0 (GET1 protein, human)
RN  - 0 (GET3 protein, human)
RN  - 0 (HSC70 Heat-Shock Proteins)
RN  - 0 (HSPA8 protein, human)
RN  - 0 (Hydrazones)
RN  - 0 (Intercellular Signaling Peptides and Proteins)
RN  - 0 (Membrane Proteins)
RN  - 0 (Membrane Transport Proteins)
RN  - 0 (Nuclear Proteins)
RN  - 0 (SEC Translocation Channels)
RN  - 0 (STATH protein, human)
RN  - 0 (Salivary Proteins and Peptides)
RN  - EC 3.6.3.16 (Arsenite Transporting ATPases)
RN  - X6Q56QN5QC (Hydroxyurea)
SB  - IM
EIN - J Cell Sci. 2012 Sep 15;125(Pt 18):4414
MH  - Amino Acid Sequence
MH  - Animals
MH  - Apelin
MH  - Arsenite Transporting ATPases/genetics/*metabolism
MH  - Dogs
MH  - Endoplasmic Reticulum/metabolism
MH  - HSC70 Heat-Shock Proteins/metabolism
MH  - Humans
MH  - Hydrazones/pharmacology
MH  - Hydroxyurea/analogs & derivatives/pharmacology
MH  - Intercellular Signaling Peptides and Proteins/*metabolism
MH  - Intracellular Membranes/metabolism
MH  - Membrane Proteins/genetics/*metabolism
MH  - Membrane Transport Proteins/*metabolism
MH  - Molecular Sequence Data
MH  - Nuclear Proteins/metabolism
MH  - *Protein Processing, Post-Translational
MH  - Protein Transport
MH  - Rabbits
MH  - SEC Translocation Channels
MH  - Salivary Proteins and Peptides/*metabolism
PMC - PMC3445324
EDAT- 2012/04/17 06:00
MHDA- 2013/05/08 06:00
PMCR- 2012/08/01
CRDT- 2012/04/17 06:00
PHST- 2012/04/17 06:00 [entrez]
PHST- 2012/04/17 06:00 [pubmed]
PHST- 2013/05/08 06:00 [medline]
PHST- 2012/08/01 00:00 [pmc-release]
AID - jcs.102608 [pii]
AID - 10.1242/jcs.102608 [doi]
PST - ppublish
SO  - J Cell Sci. 2012 Aug 1;125(Pt 15):3612-20. doi: 10.1242/jcs.102608. Epub 2012 Apr 
      14.