Cited by 95Ubiquitin and proteasome pathwaysHeat shock proteins researchCellular transport and secretion

SVIP is a novel VCP/p97-interacting protein whose expression causes cell vacuolation

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Nagahama, Masami, Suzuki, Mie, Hamada, Yuko, Hatsuzawa, Kiyotaka, Tani, Katsuko, Yamamoto, Akitsugu, Tagaya, Mitsuo·2003·Molecular Biology of the Cell

Abstract

VCP/p97 is involved in a variety of cellular processes, including membrane fusion and ubiquitin-dependent protein degradation. It has been suggested that adaptor proteins such as p47 and Ufd1p confer functional versatility to VCP/p97. To identify novel adaptors, we searched for proteins that interact specifically with VCP/p97 by using the yeast two-hybrid system, and discovered a novel VCP/p97-interacting protein named smallVCP/p97-interactingprotein (SVIP). Rat SVIP is a 76-amino acid protein that contains two putative coiled-coil regions, and potential myristoylation and palmitoylation sites at the N terminus. Binding experiments revealed that the N-terminal coiled-coil region of SVIP, and the N-terminal and subsequent ATP-binding regions (ND1 domain) of VCP/p97, interact with each other. SVIP and previously identified adaptors p47 and ufd1p interact with VCP/p97 in a mutually exclusive manner. Overexpression of full-length SVIP or a truncated mutant did not markedly affect the structure of the Golgi apparatus, but caused extensive cell vacuolation reminiscent of that seen upon the expression of VCP/p97 mutants or polyglutamine proteins in neuronal cells. The vacuoles seemed to be derived from endoplasmic reticulum membranes. These results together suggest that SVIP is a novelVCP/p97 adaptor whose function is related to the integrity of the endoplasmic reticulum.

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Authors
Nagahama, M., Suzuki, M., Hamada, Y., Hatsuzawa, K., Tani, K., Yamamoto, A., & Tagaya, M.
Affiliations
  • Tokyo University of Pharmacy and Life Sciences (JP)
  • Kansai Medical University (JP)
Venue
Molecular Biology of the Cell
Published
2003-01
Volume
14
Issue
1
Pages
262-273
ISSN
  • 1059-1524 (ISSN-L)
  • 1939-4586
OpenAlex
W2160545452
Cited by
95
References
62
Citations by year
2026: 3 · 2025: 3 · 2024: 7 · 2023: 2 · 2022: 2 · 2021: 1 · 2019: 2 · 2017: 2 · 2016: 1 · 2015: 2 · 2013: 5 · 2012: 2
FWCI
4.61
Type
journal article
Language
en
Open access
Locations
  • Molecular Biology of the Cell (publishedVersion)
  • Europe PMC (PubMed Central) (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • Uehara Memorial Foundation
  • Ministry of Education, Culture, Sports, Science and Technology
  • Japan Society for the Promotion of Science (11480183, 10215205)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
Keywords
VCP/p97, protein-protein interaction, coiled-coil domain, vacuolization, Golgi apparatus, p47phox, polyglutamine proteins, myristoylation, palmitoylation, ATP-binding domain
MeSH terms
Animals, Endoplasmic Reticulum, Nuclear Proteins, Protein Binding, Vacuoles, Protozoan Proteins, Two-Hybrid System Techniques, Rats

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