PMID- 10393181
OWN - NLM
STAT- MEDLINE
DCOM- 19990831
LR  - 20131121
IS  - 0261-4189 (Print)
IS  - 0261-4189 (Linking)
VI  - 18
IP  - 13
DP  - 1999 Jul 1
TI  - Phosphorylation by CK2 and MAPK enhances calnexin association with ribosomes.
PG  - 3655-66
AB  - Calnexin was initially identified as an endoplasmic reticulum (ER) type I
      integral membrane protein, phosphorylated on its cytosolic domain by
      ER-associated protein kinases. Although the role of the ER luminal domain of
      calnexin has been established as a constituent of the molecular chaperone
      machinery of the ER, less is known about the role of the cytosolic
      phosphorylation of calnexin. Analysis by two-dimensional phosphopeptide maps
      revealed that calnexin was in vitro phosphorylated in isolated microsomes by
      casein kinase 2 (CK2) and extracellular-signal regulated kinase-1 (ERK-1) at
      sites corresponding to those for in vivo phosphorylation. In canine pancreatic
      microsomes, synergistic phosphorylation by CK2 and ERK-1 led to increased
      association of calnexin with membrane-bound ribosomes. In vivo,
      calnexin-associated ERK-1 activity was identified by co-immunoprecipitation. This
      activity was abolished in cells expressing a dominant-negative MEK-1. Activation 
      of ERK-1 in cells by addition of serum led to a 4-fold increase in
      ribosome-associated calnexin over unstimulated cells. Taken together with studies
      revealing calnexin association with CK2 and ERK-1, a model is proposed whereby
      phosphorylation of calnexin leads to a potential increase in glycoprotein folding
      close to the translocon.
FAU - Chevet, E
AU  - Chevet E
AD  - Department of Anatomy and Cell Biology, McGill University, Montreal, Quebec, H3A 
      2B2.
FAU - Wong, H N
AU  - Wong HN
FAU - Gerber, D
AU  - Gerber D
FAU - Cochet, C
AU  - Cochet C
FAU - Fazel, A
AU  - Fazel A
FAU - Cameron, P H
AU  - Cameron PH
FAU - Gushue, J N
AU  - Gushue JN
FAU - Thomas, D Y
AU  - Thomas DY
FAU - Bergeron, J J
AU  - Bergeron JJ
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - EMBO J
JT  - The EMBO journal
JID - 8208664
RN  - 0 (Blood Proteins)
RN  - 0 (Calcium-Binding Proteins)
RN  - 0 (Recombinant Fusion Proteins)
RN  - 139873-08-8 (Calnexin)
RN  - 452VLY9402 (Serine)
RN  - EC 2.7.10.1 (Protein-Tyrosine Kinases)
RN  - EC 2.7.11.1 (Casein Kinase II)
RN  - EC 2.7.11.1 (Protein-Serine-Threonine Kinases)
RN  - EC 2.7.11.17 (Calcium-Calmodulin-Dependent Protein Kinases)
RN  - EC 2.7.11.24 (Mitogen-Activated Protein Kinase 3)
RN  - EC 2.7.11.24 (Mitogen-Activated Protein Kinases)
RN  - EC 2.7.12.2 (MAP Kinase Kinase 1)
RN  - EC 2.7.12.2 (Mitogen-Activated Protein Kinase Kinases)
SB  - IM
MH  - Animals
MH  - Blood Proteins/pharmacology
MH  - Calcium-Binding Proteins/*metabolism
MH  - Calcium-Calmodulin-Dependent Protein Kinases/*metabolism
MH  - Calnexin
MH  - Casein Kinase II
MH  - Cell Line
MH  - Cytosol/metabolism
MH  - Dogs
MH  - Endoplasmic Reticulum, Rough/drug effects/enzymology/metabolism
MH  - Enzyme Activation/drug effects
MH  - Intracellular Membranes/drug effects/enzymology/metabolism
MH  - MAP Kinase Kinase 1
MH  - Microsomes/drug effects/enzymology/metabolism
MH  - Mitogen-Activated Protein Kinase 3
MH  - *Mitogen-Activated Protein Kinase Kinases
MH  - *Mitogen-Activated Protein Kinases
MH  - Pancreas/cytology
MH  - Phosphorylation
MH  - Precipitin Tests
MH  - Protein Binding/drug effects
MH  - Protein-Serine-Threonine Kinases/genetics/*metabolism
MH  - Protein-Tyrosine Kinases/genetics/metabolism
MH  - Rats
MH  - Recombinant Fusion Proteins/metabolism
MH  - Ribosomes/drug effects/*metabolism
MH  - Serine/metabolism
PMC - PMC1171443
EDAT- 1999/07/07 00:00
MHDA- 1999/07/07 00:01
CRDT- 1999/07/07 00:00
PHST- 1999/07/07 00:00 [pubmed]
PHST- 1999/07/07 00:01 [medline]
PHST- 1999/07/07 00:00 [entrez]
AID - 10.1093/emboj/18.13.3655 [doi]
PST - ppublish
SO  - EMBO J. 1999 Jul 1;18(13):3655-66. doi: 10.1093/emboj/18.13.3655.