The pleckstrin homology domain proteins Slm1 and Slm2 are required for actin cytoskeleton organization in yeast and bind phosphatidylinositol-4,5- bisphosphate and TORC2

Maria Fadri, Alexes Daquinag, Shimei Wang, Tao Xue, Jeannette Kunz

Research output: Contribution to journalArticle

95 Citations (Scopus)

Abstract

Phosphatidylinositol-4,5-bisphosphate [PtdIns(4,5)P2] is a key second messenger that regulates actin and membrane dynamics, as well as other cellular processes. Many of the effects of PtdIns(4,5)P2 are mediated by binding to effector proteins that contain a pleckstrin homology (PH) domain. Here, we identify two novel effectors of PtdIns(4,5)P2 in the budding yeast Saccharomyces cerevisiae: the PH domain containing protein Slm1 and its homolog Slm2. Slm1 and Slm2 serve redundant roles essential for cell growth and actin cytoskeleton polarization. Slm1 and Slm2 bind PtdIns(4,5)P 2 through their PH domains. In addition, Slm1 and Slm2 physically interact with Avo2 and Bit61, two components of the TORC2 signaling complex, which mediates Tor2 signaling to the actin cytoskeleton. Together, these interactions coordinately regulate Slm1 targeting to the plasma membrane. Our results thus identify two novel effectors of PtdIns(4,5)P2 regulating cell growth and actin organization and suggest that Slm1 and Slm2 integrate inputs from the PtdIns(4,5)P2 and TORC2 to modulate polarized actin assembly and growth.

Original languageEnglish
Pages (from-to)1883-1900
Number of pages18
JournalMolecular Biology of the Cell
Volume16
Issue number4
DOIs
Publication statusPublished - Apr 2005
Externally publishedYes

Fingerprint

Phosphatidylinositol 4,5-Diphosphate
Phosphatidylinositols
Actin Cytoskeleton
Yeasts
Actins
Proteins
Growth
Saccharomycetales
Second Messenger Systems
Saccharomyces cerevisiae
Cell Membrane
TOR complex 2
Pleckstrin Homology Domains
Membranes

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics
  • Cell Biology

Cite this

The pleckstrin homology domain proteins Slm1 and Slm2 are required for actin cytoskeleton organization in yeast and bind phosphatidylinositol-4,5- bisphosphate and TORC2. / Fadri, Maria; Daquinag, Alexes; Wang, Shimei; Xue, Tao; Kunz, Jeannette.

In: Molecular Biology of the Cell, Vol. 16, No. 4, 04.2005, p. 1883-1900.

Research output: Contribution to journalArticle

@article{d078b8d0d3f94e1fa338141dd1108582,
title = "The pleckstrin homology domain proteins Slm1 and Slm2 are required for actin cytoskeleton organization in yeast and bind phosphatidylinositol-4,5- bisphosphate and TORC2",
abstract = "Phosphatidylinositol-4,5-bisphosphate [PtdIns(4,5)P2] is a key second messenger that regulates actin and membrane dynamics, as well as other cellular processes. Many of the effects of PtdIns(4,5)P2 are mediated by binding to effector proteins that contain a pleckstrin homology (PH) domain. Here, we identify two novel effectors of PtdIns(4,5)P2 in the budding yeast Saccharomyces cerevisiae: the PH domain containing protein Slm1 and its homolog Slm2. Slm1 and Slm2 serve redundant roles essential for cell growth and actin cytoskeleton polarization. Slm1 and Slm2 bind PtdIns(4,5)P 2 through their PH domains. In addition, Slm1 and Slm2 physically interact with Avo2 and Bit61, two components of the TORC2 signaling complex, which mediates Tor2 signaling to the actin cytoskeleton. Together, these interactions coordinately regulate Slm1 targeting to the plasma membrane. Our results thus identify two novel effectors of PtdIns(4,5)P2 regulating cell growth and actin organization and suggest that Slm1 and Slm2 integrate inputs from the PtdIns(4,5)P2 and TORC2 to modulate polarized actin assembly and growth.",
author = "Maria Fadri and Alexes Daquinag and Shimei Wang and Tao Xue and Jeannette Kunz",
year = "2005",
month = "4",
doi = "10.1091/mbc.E04-07-0564",
language = "English",
volume = "16",
pages = "1883--1900",
journal = "Molecular Biology of the Cell",
issn = "1059-1524",
publisher = "American Society for Cell Biology",
number = "4",

}

TY - JOUR

T1 - The pleckstrin homology domain proteins Slm1 and Slm2 are required for actin cytoskeleton organization in yeast and bind phosphatidylinositol-4,5- bisphosphate and TORC2

AU - Fadri, Maria

AU - Daquinag, Alexes

AU - Wang, Shimei

AU - Xue, Tao

AU - Kunz, Jeannette

PY - 2005/4

Y1 - 2005/4

N2 - Phosphatidylinositol-4,5-bisphosphate [PtdIns(4,5)P2] is a key second messenger that regulates actin and membrane dynamics, as well as other cellular processes. Many of the effects of PtdIns(4,5)P2 are mediated by binding to effector proteins that contain a pleckstrin homology (PH) domain. Here, we identify two novel effectors of PtdIns(4,5)P2 in the budding yeast Saccharomyces cerevisiae: the PH domain containing protein Slm1 and its homolog Slm2. Slm1 and Slm2 serve redundant roles essential for cell growth and actin cytoskeleton polarization. Slm1 and Slm2 bind PtdIns(4,5)P 2 through their PH domains. In addition, Slm1 and Slm2 physically interact with Avo2 and Bit61, two components of the TORC2 signaling complex, which mediates Tor2 signaling to the actin cytoskeleton. Together, these interactions coordinately regulate Slm1 targeting to the plasma membrane. Our results thus identify two novel effectors of PtdIns(4,5)P2 regulating cell growth and actin organization and suggest that Slm1 and Slm2 integrate inputs from the PtdIns(4,5)P2 and TORC2 to modulate polarized actin assembly and growth.

AB - Phosphatidylinositol-4,5-bisphosphate [PtdIns(4,5)P2] is a key second messenger that regulates actin and membrane dynamics, as well as other cellular processes. Many of the effects of PtdIns(4,5)P2 are mediated by binding to effector proteins that contain a pleckstrin homology (PH) domain. Here, we identify two novel effectors of PtdIns(4,5)P2 in the budding yeast Saccharomyces cerevisiae: the PH domain containing protein Slm1 and its homolog Slm2. Slm1 and Slm2 serve redundant roles essential for cell growth and actin cytoskeleton polarization. Slm1 and Slm2 bind PtdIns(4,5)P 2 through their PH domains. In addition, Slm1 and Slm2 physically interact with Avo2 and Bit61, two components of the TORC2 signaling complex, which mediates Tor2 signaling to the actin cytoskeleton. Together, these interactions coordinately regulate Slm1 targeting to the plasma membrane. Our results thus identify two novel effectors of PtdIns(4,5)P2 regulating cell growth and actin organization and suggest that Slm1 and Slm2 integrate inputs from the PtdIns(4,5)P2 and TORC2 to modulate polarized actin assembly and growth.

UR - http://www.scopus.com/inward/record.url?scp=16344385976&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=16344385976&partnerID=8YFLogxK

U2 - 10.1091/mbc.E04-07-0564

DO - 10.1091/mbc.E04-07-0564

M3 - Article

VL - 16

SP - 1883

EP - 1900

JO - Molecular Biology of the Cell

JF - Molecular Biology of the Cell

SN - 1059-1524

IS - 4

ER -