Verprolin cytokinesis function mediated by the Hof one trap domain

Ren, Gang, Wang, Juan, Brinkworth, Ross, Winsor, Barbara, Kobe, Bostjan and Munn, Alan L. (2005) Verprolin cytokinesis function mediated by the Hof one trap domain. Traffic, 6 7: 575-593. doi:10.1111/j.1600-0854.2005.00300.x


Author Ren, Gang
Wang, Juan
Brinkworth, Ross
Winsor, Barbara
Kobe, Bostjan
Munn, Alan L.
Title Verprolin cytokinesis function mediated by the Hof one trap domain
Journal name Traffic   Check publisher's open access policy
ISSN 1398-9219
Publication date 2005-01-01
Sub-type Article (original research)
DOI 10.1111/j.1600-0854.2005.00300.x
Volume 6
Issue 7
Start page 575
End page 593
Total pages 19
Place of publication Oxford
Publisher Blackwell Publishing
Collection year 2005
Language eng
Subject C1
780105 Biological sciences
270103 Protein Targeting and Signal Transduction
Abstract In budding yeast, partitioning of the cytoplasm during cytokinesis can proceed via a pathway dependent on the contractile actomyosin ring, as in other eukaryotes, or alternatively via a septum deposition pathway dependent on an SH3 domain protein, Hof1/Cyk2 (the yeast PSTPIP1 ortholog). In dividing yeast cells, Hof1 forms a ring at the bud neck distinct from the actomyosin ring, and this zone is active in septum deposition. We previously showed the yeast Wiskott-Aldrich syndrome protein (WASP)-interacting protein (WIP) ortholog, verprolin/Vrp1/End5, interacts with Hof1 and facilitates Hof1 recruitment to the bud neck. A Vrp1 fragment unable to interact with yeast WASP (Las17/Bee1), localize to the actin cytoskeleton or function in polarization of the cortical actin cytoskeleton nevertheless retains function in Hof1 recruitment and cytokinesis. Here, we show the ability of this Vrp1 fragment to bind the Hof1 SH3 domain via its Hof one trap (HOT) domain is critical for cytokinesis. The Vrp1 HOT domain consists of three tandem proline-rich motifs flanked by serines. Unexpectedly, the Hof 1 SH3 domain itself is not required for cytokinesis and indeed appears to negatively regulate cytokinesis. The Vrp1 HOT domain promotes cytokinesis by binding to the Hof 1 SH3 domain and counteracting its inhibitory effect.
Keyword Cell Cycle
Cell Division
Cell Polarity
Cortical Actin Patch
End5
Myo3
Myo5
Pch
Schizosaccharomyces Pombe Cdc15
Type I Myosin
Cell Biology
Aldrich-syndrome Protein
Yeast Actin Cytoskeleton
Saccharomyces-cerevisiae
Myosin-i
Arp2/3 Complex
Tyrosine Phosphatase
Cysteine Proteinase
Interacting Protein
Family Protein
Sh3 Domain
Cell Biology
Q-Index Code C1

 
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Created: Wed, 15 Aug 2007, 16:06:19 EST