Function
Paxillin (PXN) is involved in actin membrane attachment at sites of cell adhesion to focal adhesion domains. PXN contains a number of domains which are involved in protein-protein interactions: LD, LIM, SH2 and SH3 binding sites. LD motifs are leucine-rich sequences which begin with leucine (L) and end with aspartate (D)[1]. PXN serves as a docking protein recruiting signaling molecules to focal adhesions.
Disease
PXN has enhanced expression in several types of cancer. PXN mutations are associated with lung cancer tumor growth[2].
Structural highlights
PXN LD motifs are localized on the N-terminal region while the LIM double zinc finger domains are found at the C-terminal.
- ↑ Tumbarello DA, Brown MC, Turner CE. The paxillin LD motifs. FEBS Lett. 2002 Feb 20;513(1):114-8. PMID:11911889
- ↑ Jagadeeswaran R, Surawska H, Krishnaswamy S, Janamanchi V, Mackinnon AC, Seiwert TY, Loganathan S, Kanteti R, Reichman T, Nallasura V, Schwartz S, Faoro L, Wang YC, Girard L, Tretiakova MS, Ahmed S, Zumba O, Soulii L, Bindokas VP, Szeto LL, Gordon GJ, Bueno R, Sugarbaker D, Lingen MW, Sattler M, Krausz T, Vigneswaran W, Natarajan V, Minna J, Vokes EE, Ferguson MK, Husain AN, Salgia R. Paxillin is a target for somatic mutations in lung cancer: implications for cell growth and invasion. Cancer Res. 2008 Jan 1;68(1):132-42. doi: 10.1158/0008-5472.CAN-07-1998. PMID:18172305 doi:https://dx.doi.org/10.1158/0008-5472.CAN-07-1998
