| RRC ID |
36541
|
| Author |
Kozubowski L, Panek H, Rosenthal A, Bloecher A, DeMarini DJ, Tatchell K.
|
| Title |
A Bni4-Glc7 phosphatase complex that recruits chitin synthase to the site of bud emergence.
|
| Journal |
Mol Biol Cell
|
| Abstract |
Bni4 is a scaffold protein in the yeast Saccharomyces cerevisiae that tethers chitin synthase III to the bud neck by interacting with septin neck filaments and with Chs4, a regulatory subunit of chitin synthase III. We show herein that Bni4 is also a limiting determinant for the targeting of the type 1 serine/threonine phosphatase (Glc7) to the bud neck. Yeast cells containing a Bni4 variant that fails to associate with Glc7 fail to tether Chs4 to the neck, due in part to the failure of Bni4(V831A/F833A) to localize properly. Conversely, the Glc7-129 mutant protein fails to bind Bni4 properly and glc7-129 mutants exhibit reduced levels of Bni4 at the bud neck. Bni4 is phosphorylated in a cell cycle-dependent manner and Bni4(V831A/F833A) is both hyperphosphorylated and mislocalized in vivo. Yeast cells lacking the protein kinase Hsl1 exhibit increased levels of Bni4-GFP at the bud neck. GFP-Chs4 does not accumulate at the incipient bud site in either a bni4::TRP1 or a bni4(V831A/F833A) mutant but does mobilize to the neck at cytokinesis. Together, these results indicate that the formation of the Bni4-Glc7 complex is required for localization to the site of bud emergence and for subsequent targeting of chitin synthase.
|
| Volume |
14(1)
|
| Pages |
26-39
|
| Published |
2003-1-1
|
| DOI |
10.1091/mbc.e02-06-0373
|
| PMID |
12529424
|
| PMC |
PMC140225
|
| MeSH |
Cell Division / physiology
Chitin Synthase / metabolism*
Phosphoprotein Phosphatases / metabolism*
Protein Kinases / metabolism
Protein Phosphatase 1
Protein Serine-Threonine Kinases
Saccharomyces cerevisiae / enzymology*
Saccharomyces cerevisiae / metabolism
Saccharomyces cerevisiae Proteins / metabolism*
|
| IF |
3.791
|
| Times Cited |
54
|
|
WOS Category
|
CELL BIOLOGY
|
| Resource |
| Cellular slime molds |
|
