![]()
|
|
||||||||
J. Biol. Chem., Vol. 276, Issue 24, 21670-21677, June 15, 2001
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
,
, and
¶
From the The BAR adaptor proteins encoded by the
RVS167 and RVS161 genes from
Saccharomyces cerevisiae form a complex that regulates actin, endocytosis, and viability following starvation or osmotic stress. In this study, we identified a human homolog of
RVS161, termed BIN3 (bridging
integrator-3), and a Schizosaccharomyces pombe
homolog of RVS161, termed hob3+
(homolog of Bin3). In
human tissues, the BIN3 gene was expressed ubiquitously
except for brain. S. pombe cells lacking Hob3p were often
multinucleate and characterized by increased amounts of
calcofluor-stained material and mislocalized F-actin. For example,
while wild-type cells localized F-actin to cell ends during interphase,
hob3
Cancer Research Group, DuPont
Pharmaceuticals Company, Glenolden Laboratory, Glenolden, Pennsylvania
19036, the § Applied Biotechnology Group, DuPont
Pharmaceuticals Company, Wilmington, Delaware 19803, and ¶ The
Wistar Institute, Philadelphia, Pennsylvania 19104
mutants had F-actin patches distributed randomly
around the cell. In addition, medial F-actin rings were rarely found in
hob3
mutants. Notably, in contrast to S. cerevisiae rvs161
mutants, hob3
mutants showed
no measurable defects in endocytosis or response to osmotic stress, yet
hob3+ complemented the osmosensitivity of a
rvs161
mutant. BIN3 failed to rescue the
osmosensitivity of rvs161
, but the actin localization defects of hob3
mutants were completely rescued by
BIN3 and partially rescued by RVS161. These
findings suggest that hob3+ and BIN3 regulate
F-actin localization, like RVS161, but that other roles for
this gene have diverged somewhat during evolution.
The nucleotide sequences reported in this paper have been submitted to the GenBankTM/EBI Data Bank with accession numbers AF2717232 (human BIN3 cDNA), AA418871 (human BIN3 EST), AAF76218 (human Bin3 protein), AF271733 (murine Bin3 cDNA), AF275638 (S. pombe hob3+ cDNA), and AAF86459 (S. pombe Hob3p).
The amino acid sequence alignment in Fig. 1 including the budding yeast protein Rvs161p has been submitted to the Swiss Protein Database under Swiss-Prot accession number 25343.
To whom correspondence should be addressed. Tel.:
610-237-7847; Fax: 610-237-7937; E-mail:
george.c.prendergast@dupontpharma.com.
This article has been cited by other articles:
![]() |
G. Ren, P. Vajjhala, J. S. Lee, B. Winsor, and A. L. Munn The BAR Domain Proteins: Molding Membranes in Fission, Fusion, and Phagy Microbiol. Mol. Biol. Rev., March 1, 2006; 70(1): 37 - 120. [Abstract] [Full Text] [PDF] |
||||
![]() |
A. J. Muller, J. F. Baker, J. B. DuHadaway, K. Ge, G. Farmer, P. S. Donover, R. Meade, C. Reid, R. Grzanna, A. H. Roach, et al. Targeted Disruption of the Murine Bin1/Amphiphysin II Gene Does Not Disable Endocytosis but Results in Embryonic Cardiomyopathy with Aberrant Myofibril Formation Mol. Cell. Biol., June 15, 2003; 23(12): 4295 - 4306. [Abstract] [Full Text] [PDF] |
||||
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| All ASBMB Journals | Molecular and Cellular Proteomics |
| Journal of Lipid Research | ASBMB Today |