Pathways & interactions
Short name: Tgfb1i1/Leupaxin/TGFB1I1
Overlapping homologous superfamilies
- Leupaxin/Paxillin/TGFB1I1 (IPR017305)
- Paxillin (IPR001904)
This entry includes the transforming growth factor beta-1-induced transcript 1 (TGFB1I1, also known as Hic-5) protein, paxillin and leupaxin.
Hic-5 functions as a molecular adapter coordinating multiple protein-protein interactions at the focal adhesion complex and in the nucleus [PMID: 9597752]. Leupaxin is a transcriptional coactivator for androgen receptor (AR) and serum response factor (SRF) [PMID: 19917054].
Paxillin is a cytoskeletal protein involved in actin-membrane attachment at sites of cell adhesion to the extracellular matrix (focal adhesion) [PMID: 7534286, PMID: 7525621]. Extensive tyrosine phosphorylation occurs during integrin-mediated cell adhesion, embryonic development, fibroblast transformation and following stimulation of cells by mitogens that operate through the 7TM family of G-protein-coupled receptors [PMID: 7525621]. Paxillin binds in vitro to the focal adhesion protein vinculin, as well as to the SH3 domain of c-Src, and, when tyrosine phosphorylated, to the SH2 domain of v-Crk [PMID: 7525621]. An N-terminal region has been identified that supports the binding of both vinculin and the focal adhesion tyrosine kinase, pp125Fak [PMID: 7525621].
Paxillin is a 68 kDa protein containing multiple domains, including four tandem C-terminal LIM domains (each of which binds 2 zinc ions); an N-terminal proline-rich domain, which contains a consensus SH3 binding site; and three potential Crk-SH2 binding sites [PMID: 7534286]. The predicted structure of paxillin suggests that it is a unique cytoskeletal protein capable of interaction with a variety of intracellular signalling and structural molecules important in growth control and the regulation of cytoskeletal organisation [PMID: 7534286, PMID: 7525621].
- PIRSF037881 (Leupaxin)