Spatial-temporal reorganization of activated integrins

Cheng Han Yu, Weiwei Luo, Michael Sheetz

Research output: Contribution to journalReview article

10 Citations (Scopus)

Abstract

Integrin receptors play important roles in cell adhesion and tumor metastasis. The coupling of mechanical sensing and biochemical ligation is known to collectively regulate the activation of integrin receptors. Recently, oligomerization of activated integrins has been considered as the primordial signature of cytoskeletal remodeling and the initiation of various downstream signals, such as focal and fibrillar adhesions. However, spatio-temporal reorganization of activated integrins and associated proteins remains poorly understood. Here, we summarized the recent discovery of sequential biophysical events of integrin activation during early adhesion formation. Using the cyclic Arg-Gly-Asp (RGD) peptide as a mobile ligand on supported lipid membranes, a series of previously unreported events were observed following integrin avb3 clustering and cell spreading, including a long-range lateral translocation of the integrin clusters. With initial clustering, localized actin polymerization occurred in a Src family kinase dependent manner. Clustering of liganded integrins recruits various adaptor proteins and serves as a reaction core for mechanobiological activities. In addition, there are future possibilities to investigate the role of other synergetic interactions with the activated integrin receptors.

Original languageEnglish (US)
Pages (from-to)280-284
Number of pages5
JournalCell Adhesion and Migration
Volume6
Issue number3
DOIs
StatePublished - Jan 1 2012
Externally publishedYes

Fingerprint

Integrins
Cluster Analysis
Focal Adhesions
src-Family Kinases
Membrane Lipids
Cell Adhesion
Polymerization
Ligation
Actins
Proteins
Neoplasm Metastasis
Ligands

Keywords

  • Actin polymerization
  • Integrin
  • RGD peptide
  • Src family kinase
  • Supported lipid membrane
  • Synergy receptor
  • Tumor metastasis

ASJC Scopus subject areas

  • Cellular and Molecular Neuroscience
  • Cell Biology

Cite this

Spatial-temporal reorganization of activated integrins. / Yu, Cheng Han; Luo, Weiwei; Sheetz, Michael.

In: Cell Adhesion and Migration, Vol. 6, No. 3, 01.01.2012, p. 280-284.

Research output: Contribution to journalReview article

Yu, Cheng Han ; Luo, Weiwei ; Sheetz, Michael. / Spatial-temporal reorganization of activated integrins. In: Cell Adhesion and Migration. 2012 ; Vol. 6, No. 3. pp. 280-284.
@article{6078dd45917c44569a62bba464982c06,
title = "Spatial-temporal reorganization of activated integrins",
abstract = "Integrin receptors play important roles in cell adhesion and tumor metastasis. The coupling of mechanical sensing and biochemical ligation is known to collectively regulate the activation of integrin receptors. Recently, oligomerization of activated integrins has been considered as the primordial signature of cytoskeletal remodeling and the initiation of various downstream signals, such as focal and fibrillar adhesions. However, spatio-temporal reorganization of activated integrins and associated proteins remains poorly understood. Here, we summarized the recent discovery of sequential biophysical events of integrin activation during early adhesion formation. Using the cyclic Arg-Gly-Asp (RGD) peptide as a mobile ligand on supported lipid membranes, a series of previously unreported events were observed following integrin avb3 clustering and cell spreading, including a long-range lateral translocation of the integrin clusters. With initial clustering, localized actin polymerization occurred in a Src family kinase dependent manner. Clustering of liganded integrins recruits various adaptor proteins and serves as a reaction core for mechanobiological activities. In addition, there are future possibilities to investigate the role of other synergetic interactions with the activated integrin receptors.",
keywords = "Actin polymerization, Integrin, RGD peptide, Src family kinase, Supported lipid membrane, Synergy receptor, Tumor metastasis",
author = "Yu, {Cheng Han} and Weiwei Luo and Michael Sheetz",
year = "2012",
month = "1",
day = "1",
doi = "10.4161/cam.20753",
language = "English (US)",
volume = "6",
pages = "280--284",
journal = "Cell Adhesion and Migration",
issn = "1933-6918",
publisher = "Landes Bioscience",
number = "3",

}

TY - JOUR

T1 - Spatial-temporal reorganization of activated integrins

AU - Yu, Cheng Han

AU - Luo, Weiwei

AU - Sheetz, Michael

PY - 2012/1/1

Y1 - 2012/1/1

N2 - Integrin receptors play important roles in cell adhesion and tumor metastasis. The coupling of mechanical sensing and biochemical ligation is known to collectively regulate the activation of integrin receptors. Recently, oligomerization of activated integrins has been considered as the primordial signature of cytoskeletal remodeling and the initiation of various downstream signals, such as focal and fibrillar adhesions. However, spatio-temporal reorganization of activated integrins and associated proteins remains poorly understood. Here, we summarized the recent discovery of sequential biophysical events of integrin activation during early adhesion formation. Using the cyclic Arg-Gly-Asp (RGD) peptide as a mobile ligand on supported lipid membranes, a series of previously unreported events were observed following integrin avb3 clustering and cell spreading, including a long-range lateral translocation of the integrin clusters. With initial clustering, localized actin polymerization occurred in a Src family kinase dependent manner. Clustering of liganded integrins recruits various adaptor proteins and serves as a reaction core for mechanobiological activities. In addition, there are future possibilities to investigate the role of other synergetic interactions with the activated integrin receptors.

AB - Integrin receptors play important roles in cell adhesion and tumor metastasis. The coupling of mechanical sensing and biochemical ligation is known to collectively regulate the activation of integrin receptors. Recently, oligomerization of activated integrins has been considered as the primordial signature of cytoskeletal remodeling and the initiation of various downstream signals, such as focal and fibrillar adhesions. However, spatio-temporal reorganization of activated integrins and associated proteins remains poorly understood. Here, we summarized the recent discovery of sequential biophysical events of integrin activation during early adhesion formation. Using the cyclic Arg-Gly-Asp (RGD) peptide as a mobile ligand on supported lipid membranes, a series of previously unreported events were observed following integrin avb3 clustering and cell spreading, including a long-range lateral translocation of the integrin clusters. With initial clustering, localized actin polymerization occurred in a Src family kinase dependent manner. Clustering of liganded integrins recruits various adaptor proteins and serves as a reaction core for mechanobiological activities. In addition, there are future possibilities to investigate the role of other synergetic interactions with the activated integrin receptors.

KW - Actin polymerization

KW - Integrin

KW - RGD peptide

KW - Src family kinase

KW - Supported lipid membrane

KW - Synergy receptor

KW - Tumor metastasis

UR - http://www.scopus.com/inward/record.url?scp=84864920732&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84864920732&partnerID=8YFLogxK

U2 - 10.4161/cam.20753

DO - 10.4161/cam.20753

M3 - Review article

VL - 6

SP - 280

EP - 284

JO - Cell Adhesion and Migration

JF - Cell Adhesion and Migration

SN - 1933-6918

IS - 3

ER -