Tensin

Research output: Contribution to journalArticle

136 Citations (Scopus)

Abstract

Tensin is a cytoplasmic phosphoprotein that localized to integrin-mediated focal adhesions. It binds to actin filaments and contains a phosphotyrosine- binding (PTB) domain, which interacts with the cytoplasmic tails of β integrin. These interactions allow tensin to link actin filaments to integrin receptors. In addition, tensin has an Src Homology 2 (SH2) domain capable of interacting with tyrosine-phosphorylated proteins. Furthermore, several factors induce tyrosine phosphorylation of tensin. Thus, tensin functions as a platform for dis/assembly of signaling complexes at focal adhesions by recruiting tyrosine-phosphorylated signaling molecules through the SH2 domain, and also by providing interaction sites for other SH2-containing proteins. Analysis of knockout mice has demonstrated critical roles of tensin in renal function, muscle regeneration, and cell migration. Therefore, tensin and its downstream signaling molecules may be targets for therapeutic interventions in renal disease, wound healing and cancer.

Original languageEnglish (US)
Pages (from-to)31-34
Number of pages4
JournalInternational Journal of Biochemistry and Cell Biology
Volume36
Issue number1
DOIs
StatePublished - Jan 2004

Fingerprint

Integrins
Tyrosine
Actins
Adhesion
Phosphotyrosine
Phosphorylation
Molecules
Phosphoproteins
Focal Adhesions
src Homology Domains
Muscle
Actin Cytoskeleton
Proteins
Kidney
Tensins
Knockout Mice
Wound Healing
Muscle Cells
Cell Movement
Tail

Keywords

  • Focal adhesion
  • PTB domain
  • SH2 domain
  • Tensin

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology

Cite this

Tensin. / Lo, Su Hao.

In: International Journal of Biochemistry and Cell Biology, Vol. 36, No. 1, 01.2004, p. 31-34.

Research output: Contribution to journalArticle

@article{c6cc1fa27c40417389a55c478356408b,
title = "Tensin",
abstract = "Tensin is a cytoplasmic phosphoprotein that localized to integrin-mediated focal adhesions. It binds to actin filaments and contains a phosphotyrosine- binding (PTB) domain, which interacts with the cytoplasmic tails of β integrin. These interactions allow tensin to link actin filaments to integrin receptors. In addition, tensin has an Src Homology 2 (SH2) domain capable of interacting with tyrosine-phosphorylated proteins. Furthermore, several factors induce tyrosine phosphorylation of tensin. Thus, tensin functions as a platform for dis/assembly of signaling complexes at focal adhesions by recruiting tyrosine-phosphorylated signaling molecules through the SH2 domain, and also by providing interaction sites for other SH2-containing proteins. Analysis of knockout mice has demonstrated critical roles of tensin in renal function, muscle regeneration, and cell migration. Therefore, tensin and its downstream signaling molecules may be targets for therapeutic interventions in renal disease, wound healing and cancer.",
keywords = "Focal adhesion, PTB domain, SH2 domain, Tensin",
author = "Lo, {Su Hao}",
year = "2004",
month = "1",
doi = "10.1016/S1357-2725(03)00171-7",
language = "English (US)",
volume = "36",
pages = "31--34",
journal = "International Journal of Biochemistry and Cell Biology",
issn = "1357-2725",
publisher = "Elsevier Limited",
number = "1",

}

TY - JOUR

T1 - Tensin

AU - Lo, Su Hao

PY - 2004/1

Y1 - 2004/1

N2 - Tensin is a cytoplasmic phosphoprotein that localized to integrin-mediated focal adhesions. It binds to actin filaments and contains a phosphotyrosine- binding (PTB) domain, which interacts with the cytoplasmic tails of β integrin. These interactions allow tensin to link actin filaments to integrin receptors. In addition, tensin has an Src Homology 2 (SH2) domain capable of interacting with tyrosine-phosphorylated proteins. Furthermore, several factors induce tyrosine phosphorylation of tensin. Thus, tensin functions as a platform for dis/assembly of signaling complexes at focal adhesions by recruiting tyrosine-phosphorylated signaling molecules through the SH2 domain, and also by providing interaction sites for other SH2-containing proteins. Analysis of knockout mice has demonstrated critical roles of tensin in renal function, muscle regeneration, and cell migration. Therefore, tensin and its downstream signaling molecules may be targets for therapeutic interventions in renal disease, wound healing and cancer.

AB - Tensin is a cytoplasmic phosphoprotein that localized to integrin-mediated focal adhesions. It binds to actin filaments and contains a phosphotyrosine- binding (PTB) domain, which interacts with the cytoplasmic tails of β integrin. These interactions allow tensin to link actin filaments to integrin receptors. In addition, tensin has an Src Homology 2 (SH2) domain capable of interacting with tyrosine-phosphorylated proteins. Furthermore, several factors induce tyrosine phosphorylation of tensin. Thus, tensin functions as a platform for dis/assembly of signaling complexes at focal adhesions by recruiting tyrosine-phosphorylated signaling molecules through the SH2 domain, and also by providing interaction sites for other SH2-containing proteins. Analysis of knockout mice has demonstrated critical roles of tensin in renal function, muscle regeneration, and cell migration. Therefore, tensin and its downstream signaling molecules may be targets for therapeutic interventions in renal disease, wound healing and cancer.

KW - Focal adhesion

KW - PTB domain

KW - SH2 domain

KW - Tensin

UR - http://www.scopus.com/inward/record.url?scp=0242285572&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0242285572&partnerID=8YFLogxK

U2 - 10.1016/S1357-2725(03)00171-7

DO - 10.1016/S1357-2725(03)00171-7

M3 - Article

C2 - 14592531

AN - SCOPUS:0242285572

VL - 36

SP - 31

EP - 34

JO - International Journal of Biochemistry and Cell Biology

JF - International Journal of Biochemistry and Cell Biology

SN - 1357-2725

IS - 1

ER -