QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

Vol. 16, Issue 8, 3455-3466, August 2005

This Article Full Text Full Text (PDF) Supplemental Videos All Versions of this Article: E04-09-0764v1 16/8/3455    most recent Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Kozubowski, L. Articles by Tatchell, K. Search for Related Content PubMed PubMed Citation Articles by Kozubowski, L. Articles by Tatchell, K.

Role of the Septin Ring in the Asymmetric Localization of Proteins at the Mother-Bud Neck in Saccharomyces cerevisiae

Department of Biochemistry and Molecular Biology, Louisiana State University Health Sciences Center, Shreveport, LA 71130

Submitted September 1, 2004; Accepted May 11, 2005
Monitoring Editor: John Pringle

In the yeast Saccharomyces cerevisiae, septins form a scaffold in the shape of a ring at the future budding site that rearranges into a collar at the mother-bud neck. Many proteins bind asymmetrically to the septin collar. We found that the protein Bni4-CFP was located on the exterior of the septin ring before budding and on the mother side of the collar after budding, whereas the protein kinase Kcc4-YFP was located on the interior of the septin ring before budding and moved into the bud during the formation of the septin collar. Unbudded cells treated with the actin inhibitor latrunculin-A assembled cortical caps of septins on which Bni4-CFP and Kcc4-YFP colocalized. Bni4-CFP and Kcc4-YFP also colocalized on cortical caps of septins found in strains deleted for the genes encoding the GTPase activating proteins of Cdc42 (RGA1, RGA2, and BEM3). However, Bni4-CFP and Kcc4-YFP were still partially separated in mutants (gin4, elm1, cla4, and cdc3-1) in which septin morphology was severely disrupted in other ways. These observations provide clues to the mechanisms for the asymmetric localization of septin-associated proteins.

Abbreviations used: Lat-A, latrunculin A.

The online version of this article contains supplemental material at MBC Online (http://www.molbiolcell.org).

^* Present address: Department of Pharmacology and Cancer Biology, Duke University Medical Center, Durham, NC 27710.

Address correspondence to: Kelly Tatchell (ktatch{at}lsuhsc.edu).

This article has been cited by other articles:

				J. R. Larson, J. P. Bharucha, S. Ceaser, J. Salamon, C. J. Richardson, S. M. Rivera, and K. Tatchell Protein Phosphatase Type 1 Directs Chitin Synthesis at the Bud Neck in Saccharomyces cerevisiae Mol. Biol. Cell, July 1, 2008; 19(7): 3040 - 3051. [Abstract] [Full Text] [PDF]

				A. Gonzalez-Novo, J. Correa-Bordes, L. Labrador, M. Sanchez, C. R. Vazquez de Aldana, and J. Jimenez Sep7 Is Essential to Modify Septin Ring Dynamics and Inhibit Cell Separation during Candida albicans Hyphal Growth Mol. Biol. Cell, April 1, 2008; 19(4): 1509 - 1518. [Abstract] [Full Text] [PDF]

				C. Wang and R. J. St Leger The MAD1 Adhesin of Metarhizium anisopliae Links Adhesion with Blastospore Production and Virulence to Insects, and the MAD2 Adhesin Enables Attachment to Plants Eukaryot. Cell, May 1, 2007; 6(5): 808 - 816. [Abstract] [Full Text] [PDF]

				H.-O. Park and E. Bi Central Roles of Small GTPases in the Development of Cell Polarity in Yeast and Beyond Microbiol. Mol. Biol. Rev., March 1, 2007; 71(1): 48 - 96. [Abstract] [Full Text] [PDF]

				M. Iwase, J. Luo, S. Nagaraj, M. Longtine, H. B. Kim, B. K. Haarer, C. Caruso, Z. Tong, J. R. Pringle, and E. Bi Role of a Cdc42p Effector Pathway in Recruitment of the Yeast Septins to the Presumptive Bud Site Mol. Biol. Cell, March 1, 2006; 17(3): 1110 - 1125. [Abstract] [Full Text] [PDF]