PMID- 10469658
OWN - NLM
STAT- MEDLINE
DCOM- 19991028
LR  - 20091214
IS  - 0261-4189 (Print)
IS  - 0261-4189 (Linking)
VI  - 18
IP  - 17
DP  - 1999 Sep 1
TI  - Control of glycosylation of MHC class II-associated invariant chain by
      translocon-associated RAMP4.
PG  - 4804-15
AB  - Protein translocation across the membrane of the endoplasmic reticulum (ER)
      proceeds through a proteinaceous translocation machinery, the translocon. To
      identify components that may regulate translocation by interacting with nascent
      polypeptides in the translocon, we used site-specific photo-crosslinking. We
      found that a region C-terminal of the two N-glycosylation sites of the MHC class 
      II-associated invariant chain (Ii) interacts specifically with the
      ribosome-associated membrane protein 4 (RAMP4). RAMP4 is a small, tail-anchored
      protein of 66 amino acid residues that is homologous to the yeast YSY6 protein.
      YSY6 suppresses a secretion defect of a secY mutant in Escherichia coli. The
      interaction of RAMP4 with Ii occurred when nascent Ii chains reached a length of 
      170 amino acid residues and persisted until Ii chain completion, suggesting
      translocational pausing. Site-directed mutagenesis revealed that the region of Ii
      interacting with RAMP4 contains essential hydrophobic amino acid residues.
      Exchange of these residues for serines led to a reduced interaction with RAMP4
      and inefficient N-glycosylation. We propose that RAMP4 controls modification of
      Ii and possibly also of other secretory and membrane proteins containing specific
      RAMP4-interacting sequences. Efficient or variable glycosylation of Ii may
      contribute to its capacity to modulate antigen presentation by MHC class II
      molecules.
FAU - Schroder, K
AU  - Schroder K
AD  - Zentrum fur Molekulare Biologie der Universitat Heidelberg (ZMBH), Postfach
      106249, 69052 Heidelberg, Germany.
FAU - Martoglio, B
AU  - Martoglio B
FAU - Hofmann, M
AU  - Hofmann M
FAU - Holscher, C
AU  - Holscher C
FAU - Hartmann, E
AU  - Hartmann E
FAU - Prehn, S
AU  - Prehn S
FAU - Rapoport, T A
AU  - Rapoport TA
FAU - Dobberstein, B
AU  - Dobberstein B
LA  - eng
SI  - GENBANK/AJ238236
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - EMBO J
JT  - The EMBO journal
JID - 8208664
RN  - 0 (Antigens, Differentiation, B-Lymphocyte)
RN  - 0 (DNA, Complementary)
RN  - 0 (Histocompatibility Antigens Class II)
RN  - 0 (Membrane Proteins)
RN  - 0 (Serp1 protein, rat)
RN  - 0 (invariant chain)
SB  - IM
EIN - EMBO J 2002 Dec 16;21(24):6954
MH  - Amino Acid Sequence
MH  - Animals
MH  - Antigens, Differentiation, B-Lymphocyte/*metabolism
MH  - DNA, Complementary/metabolism
MH  - Glycosylation
MH  - Histocompatibility Antigens Class II/*metabolism
MH  - Humans
MH  - Membrane Proteins/*metabolism
MH  - Mice
MH  - Models, Biological
MH  - Molecular Sequence Data
MH  - Mutagenesis
MH  - Precipitin Tests
MH  - Protein Binding
MH  - Protein Biosynthesis
MH  - Rats
MH  - Ribosomes/*metabolism
MH  - Sequence Homology, Amino Acid
MH  - Time Factors
PMC - PMC1171552
EDAT- 1999/09/02 00:00
MHDA- 1999/09/02 00:01
CRDT- 1999/09/02 00:00
PHST- 1999/09/02 00:00 [pubmed]
PHST- 1999/09/02 00:01 [medline]
PHST- 1999/09/02 00:00 [entrez]
AID - 10.1093/emboj/18.17.4804 [doi]
PST - ppublish
SO  - EMBO J. 1999 Sep 1;18(17):4804-15. doi: 10.1093/emboj/18.17.4804.