Journal
JOURNAL OF CELL SCIENCE
Volume 125, Issue 23, Pages 5647-5657Publisher
COMPANY OF BIOLOGISTS LTD
DOI: 10.1242/jcs.103291
Keywords
PDZ domain protein; Zasp; Adhesion receptor; Extracellular matrix; Integrin activation; Muscle attachment
Categories
Funding
- Canada Foundation for Innovation [9607]
- Canadian Institutes of Health Research [MOP-74716, MOP-93727]
- National Institutes of Health [HL089433, GM068600]
- National Science Foundation [DGE-1122492]
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Integrins are heterodimeric adhesion receptors that link the extracellular matrix (ECM) to the cytoskeleton. Binding of the scaffold protein, talin, to the cytoplasmic tail of beta-integrin causes a conformational change of the extracellular domains of the integrin heterodimer, thus allowing high-affinity binding of ECM ligands. This essential process is called integrin activation. Here we report that the Z-band alternatively spliced PDZ-motif-containing protein (Zasp) cooperates with talin to activate alpha 5 beta 1 integrins in mammalian tissue culture and alpha PS2 beta PS integrins in Drosophila. Zasp is a PDZ-LIM-domain-containing protein mutated in human cardiomyopathies previously thought to function primarily in assembly and maintenance of the muscle contractile machinery. Notably, Zasp is the first protein shown to co-activate alpha 5 beta 1 integrins with talin and appears to do so in a manner distinct from known alpha IIb beta 3 integrin co-activators.
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