ILK, PINCH and parvin: the tIPP of integrin signalling.
The ternary complex of integrin-linked kinase (ILK), PINCH and parvin functions as a signalling platform for integrins by interfacing with the actin cytoskeleton and many diverse signalling pathways. All these proteins have synergistic functions at focal adhesions, but recent work has indicated that these proteins might also have separate roles within a cell. They function as regulators of gene transcription or cell-cell adhesion.
Department of Molecular Medicine, Max-Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsreid, Germany. legate@biochem.mpg.de
Kyle R
KR
Legate
Eloi
E
Montañez
Oliver
O
Kudlacek
Reinhard
R
Fässler
D000185:Actinin / Q000378:metabolism*; D000595:Amino Acid Sequence; D000818:Animals; D004268:DNA-Binding Proteins / Q000378:metabolism*; D006801:Humans; D016023:Integrins / Q000378:metabolism*; D051379:Mice; D008969:Molecular Sequence Data; D017346:Protein Serine-Threonine Kinases / Q000378:metabolism*; D015398:Signal Transduction; D016335:Zinc Fingers; D000099200:Scaffold Protein ILK
D000185:Actinin; D004268:DNA-Binding Proteins; D016023:Integrins; D017346:Protein Serine-Threonine Kinases; D000099200:Scaffold Protein ILK