Stress-associated endoplasmic reticulum protein 1 (SERP1)/ribosome- associated membrane protein 4 (RAMP4) stabilizes membrane proteins during stress and facilitates subsequent glycosylation

Atsushi Yamaguchi, Osamu Hori, David Stern, Enno Hartmann, Satoshi Ogawa, Masaya Tohyama

Research output: Contribution to journalArticle

79 Citations (Scopus)

Abstract

Application of differential display to cultured rat astrocytes subjected to hypoxia allowed cloning of a novel cDNA, termed stress-associated endoplasmic reticulum protein 1 (SERP1). Expression of SERP1 was enhanced in vitro by hypoxia and/or reoxygenation or other forms of stress, causing accumulation of unfolded proteins in endoplasmic reticulum (ER) stress, and in vivo by middle cerebral artery occlusion in rats. The SERP1 cDNA encodes a 66-amino acid polypeptide which was found to be identical to ribosome- associated membrane protein 4 (RAMP4) and bearing 29% identity to yeast suppressor of SecY 6 protein (YSY6p), suggesting participation in pathways controlling membrane protein biogenesis at ER. In cultured 293 cells subjected to ER stress, overexpression of SERP1/RAMP4 suppressed aggregation and/or degradation of newly synthesized integral membrane proteins, and subsequently, facilitated their glycosylation when the stress was removed. SERP1/RAMP4 interacted with Sec61α and Sec61β, which are subunits of translocon, and a molecular chaperon calnexin. Furthermore, Sec61α and Sec61β, but not SERP1/RAMP4, were found to associate with newly synthesized integral membrane proteins under stress. These results suggest that stabilization of membrane proteins in response to stress involves the concerted action of a rescue unit in the ER membrane comprised of SERP1/RAMP4, other components of translocon, and molecular chaperons in ER.

Original languageEnglish (US)
Pages (from-to)1195-1204
Number of pages10
JournalJournal of Cell Biology
Volume147
Issue number6
DOIs
StatePublished - Dec 13 1999

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Endoplasmic Reticulum Stress
Ribosomes
Glycosylation
Membrane Proteins
Proteins
Endoplasmic Reticulum
Molecular Chaperones
Complementary DNA
Calnexin
Protein Unfolding
Middle Cerebral Artery Infarction
Astrocytes
Organism Cloning
Cultured Cells
Yeasts
Amino Acids
Peptides
Membranes

All Science Journal Classification (ASJC) codes

  • Cell Biology

Cite this

Stress-associated endoplasmic reticulum protein 1 (SERP1)/ribosome- associated membrane protein 4 (RAMP4) stabilizes membrane proteins during stress and facilitates subsequent glycosylation. / Yamaguchi, Atsushi; Hori, Osamu; Stern, David; Hartmann, Enno; Ogawa, Satoshi; Tohyama, Masaya.

In: Journal of Cell Biology, Vol. 147, No. 6, 13.12.1999, p. 1195-1204.

Research output: Contribution to journalArticle

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