A novel function of VCP (valosin-containing protein; p97) in the control of N-glycosylation of proteins in the endoplasmic reticulum.

A novel function of VCP (valosin-containing protein; p97) in the control of N-glycosylation of proteins in the endoplasmic reticulum. Research Abstract Details 

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A novel function of VCP (valosin-containing protein; p97) in the control of N-glycosylation of proteins in the endoplasmic reticulum. Abstract Text:

Agnieszka Lass,Elizabeth McConnell,Dominika Nowis,Yehia Mechref,Pilsoo Kang,Milos V Novotny,Cezary ,

alpha-Chain of T-cell receptor (TCR) is a typical ERAD (ER-associated degradation) substrate degraded in the absence of other TCR subunits. Depletion of derlin 1 fails to induce accumulation of alphaTCR despite inducing accumulation of alpha1-antitrypsin, another ERAD substrate. Furthermore, while depletion of VCP does not affect levels of alpha1-antitrypsin, it induces an increase in levels of alphaTCR. RNAi of VCP induces preferential accumulation of alphaTCR with less mannose residues, suggesting its retention within the ER. Mass spectrometric analysis of cellular N-linked glycans revealed that depletion of VCP decreases the level of high-mannose glycoproteins, increases the levels of truncated low-mannose glycoproteins and induces changes in the abundance of complex glycans assembled in post-ER compartments. Since proteasome inhibition was unable to mimic those changes, they cannot be regarded as a simple consequence of inhibited ERAD but represent a complex effect of VCP on the function of the ER.

A novel function of VCP (valosin-containing protein; p97) in the control of N-glycosylation of proteins in the endoplasmic reticulum. Publishing Authors By Initials

A Lass,E McConnell,D Nowis,Y Mechref,P Kang,MV Novotny,C ,

For similar peptides: proteinase inhibitory proteins, secretory: alpha 1-antitrypsin research abstracts see: peptides: proteinase inhibitory proteins, secretory: alpha 1-antitrypsin research

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A novel function of VCP (valosin-containing protein; p97) in the control of N-glycosylation of proteins in the endoplasmic reticulum. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Archives of biochemistry and biophysics

VOLUME: 462

Page Numbers: 62-73

Journal Abbreviation: Arch. Biochem. Biophys.

ISSN: 0003-9861

DAY: 25

MONTH: 04

YEAR: 2007

A novel function of VCP (valosin-containing protein; p97) in the control of N-glycosylation of proteins in the endoplasmic reticulum. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 372430

A novel function of VCP (valosin-containing protein; p97) in the control of N-glycosylation of proteins in the endoplasmic reticulum. Keywords Mesh Terms:

KEYWORDS: alpha 1-Antitrypsin

MESH TERMS: chemistry

Chemical & Substance for Abstract: A novel function of VCP (valosin-containing protein; p97) in the control of N-glycosylation of proteins in the endoplasmic reticulum. Information

Substance Name: Adenosine Triphosphatases

Registry Number: EC 3.6.1.-

Grant and Affiliation Information for A novel function of VCP (valosin-containing protein; p97) in the control of N-glycosylation of proteins in the endoplasmic reticulum.

AFFILIATION: Department of Anatomy and Cell Biology, Indiana University School of Medicine-Evansville, Evansville, IN 47712, USA.

Country: United States

AGENCY: United States NCRR

GRANT: RR018942

ACRONYM: RR

MEDLINETA: Arch Biochem Biophys

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