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Vol. 14, Issue 1, 262-273, January 2003
and
*School of Life Science, Tokyo University of Pharmacy and
Life Science, Hachioji, Tokyo 192-0392, Japan; and
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 small
VCP/p97-interacting
protein (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.
Department of Physiology, Kansai Medical
University, Moriguchi, Osaka 570-8506, Japan
These authors contributed equally to this work.
§
Corresponding author. E-mail address:
tagaya{at}ls.toyaku.ac.jp.
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