Phosphatidylinositol 4,5-bisphosphate functions as a second messenger that regulates cytoskeleton-plasma membrane adhesion

Drazen Raucher, Thomas Stauffer, Wen Chen, Kang Shen, Shuling Guo, John D. York, Michael Sheetz, Tobias Meyer

Research output: Contribution to journalArticle

524 Citations (Scopus)

Abstract

Binding interactions between the plasma membrane and the cytoskeleton define cell functions such as cell shape, formation of cell processes, cell movement, and endocytosis. Here we use optical tweezers tether force measurements and show that plasma membrane phosphatidylinositol 4,5- bisphosphate (PIP2) acts as a second messenger that regulates the adhesion energy between the cytoskeleton and the plasma membrane. Receptor stimuli that hydrolyze PIP2 lowered adhesion energy, a process that could be mimicked by expressing PH domains that sequester PIP2 or by targeting a 5'-PIP2- phosphatase to the plasma membrane to selectively lower plasma membrane PIP2 concentration. Our study suggests that plasma membrane PIP2 controls dynamic membrane functions and cell shape by locally increasing and decreasing the adhesion between the actin-based cortical cytoskeleton and the plasma membrane.

Original languageEnglish (US)
Pages (from-to)221-228
Number of pages8
JournalCell
Volume100
Issue number2
DOIs
StatePublished - Jan 21 2000
Externally publishedYes

Fingerprint

Second Messenger Systems
Cell membranes
Phosphatidylinositols
Cytoskeleton
Adhesion
Cell Membrane
Cell Shape
Cells
Optical Tweezers
Optical tweezers
Force measurement
Endocytosis
Phosphoric Monoester Hydrolases
Cell Movement
Actins
Membranes

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

Cite this

Phosphatidylinositol 4,5-bisphosphate functions as a second messenger that regulates cytoskeleton-plasma membrane adhesion. / Raucher, Drazen; Stauffer, Thomas; Chen, Wen; Shen, Kang; Guo, Shuling; York, John D.; Sheetz, Michael; Meyer, Tobias.

In: Cell, Vol. 100, No. 2, 21.01.2000, p. 221-228.

Research output: Contribution to journalArticle

Raucher, Drazen ; Stauffer, Thomas ; Chen, Wen ; Shen, Kang ; Guo, Shuling ; York, John D. ; Sheetz, Michael ; Meyer, Tobias. / Phosphatidylinositol 4,5-bisphosphate functions as a second messenger that regulates cytoskeleton-plasma membrane adhesion. In: Cell. 2000 ; Vol. 100, No. 2. pp. 221-228.
@article{e75d52fc94074dbd9e92b55baf60fc1d,
title = "Phosphatidylinositol 4,5-bisphosphate functions as a second messenger that regulates cytoskeleton-plasma membrane adhesion",
abstract = "Binding interactions between the plasma membrane and the cytoskeleton define cell functions such as cell shape, formation of cell processes, cell movement, and endocytosis. Here we use optical tweezers tether force measurements and show that plasma membrane phosphatidylinositol 4,5- bisphosphate (PIP2) acts as a second messenger that regulates the adhesion energy between the cytoskeleton and the plasma membrane. Receptor stimuli that hydrolyze PIP2 lowered adhesion energy, a process that could be mimicked by expressing PH domains that sequester PIP2 or by targeting a 5'-PIP2- phosphatase to the plasma membrane to selectively lower plasma membrane PIP2 concentration. Our study suggests that plasma membrane PIP2 controls dynamic membrane functions and cell shape by locally increasing and decreasing the adhesion between the actin-based cortical cytoskeleton and the plasma membrane.",
author = "Drazen Raucher and Thomas Stauffer and Wen Chen and Kang Shen and Shuling Guo and York, {John D.} and Michael Sheetz and Tobias Meyer",
year = "2000",
month = "1",
day = "21",
doi = "10.1016/S0092-8674(00)81560-3",
language = "English (US)",
volume = "100",
pages = "221--228",
journal = "Cell",
issn = "0092-8674",
publisher = "Cell Press",
number = "2",

}

TY - JOUR

T1 - Phosphatidylinositol 4,5-bisphosphate functions as a second messenger that regulates cytoskeleton-plasma membrane adhesion

AU - Raucher, Drazen

AU - Stauffer, Thomas

AU - Chen, Wen

AU - Shen, Kang

AU - Guo, Shuling

AU - York, John D.

AU - Sheetz, Michael

AU - Meyer, Tobias

PY - 2000/1/21

Y1 - 2000/1/21

N2 - Binding interactions between the plasma membrane and the cytoskeleton define cell functions such as cell shape, formation of cell processes, cell movement, and endocytosis. Here we use optical tweezers tether force measurements and show that plasma membrane phosphatidylinositol 4,5- bisphosphate (PIP2) acts as a second messenger that regulates the adhesion energy between the cytoskeleton and the plasma membrane. Receptor stimuli that hydrolyze PIP2 lowered adhesion energy, a process that could be mimicked by expressing PH domains that sequester PIP2 or by targeting a 5'-PIP2- phosphatase to the plasma membrane to selectively lower plasma membrane PIP2 concentration. Our study suggests that plasma membrane PIP2 controls dynamic membrane functions and cell shape by locally increasing and decreasing the adhesion between the actin-based cortical cytoskeleton and the plasma membrane.

AB - Binding interactions between the plasma membrane and the cytoskeleton define cell functions such as cell shape, formation of cell processes, cell movement, and endocytosis. Here we use optical tweezers tether force measurements and show that plasma membrane phosphatidylinositol 4,5- bisphosphate (PIP2) acts as a second messenger that regulates the adhesion energy between the cytoskeleton and the plasma membrane. Receptor stimuli that hydrolyze PIP2 lowered adhesion energy, a process that could be mimicked by expressing PH domains that sequester PIP2 or by targeting a 5'-PIP2- phosphatase to the plasma membrane to selectively lower plasma membrane PIP2 concentration. Our study suggests that plasma membrane PIP2 controls dynamic membrane functions and cell shape by locally increasing and decreasing the adhesion between the actin-based cortical cytoskeleton and the plasma membrane.

UR - http://www.scopus.com/inward/record.url?scp=0034695461&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0034695461&partnerID=8YFLogxK

U2 - 10.1016/S0092-8674(00)81560-3

DO - 10.1016/S0092-8674(00)81560-3

M3 - Article

VL - 100

SP - 221

EP - 228

JO - Cell

JF - Cell

SN - 0092-8674

IS - 2

ER -