Pfam Domain Structure

From PXN (chicken) - phosphorylation sites added via direct mapping

Members of the Paxillin Family

1: PXN »	Human	Mouse	Rat	Chicken	Fly	Worm
CMKB	PXN	Pxn	Pxn	PXN	Pax	pxl-1
Entrez Gene	5829	19303	360820	395832	35215	175831
Uniprot	PAXI_HUMAN	PAXI_MOUSE	PAXI_RAT	PAXI_CHICK	-	PXL1_CAEEL
OMIM	602505	-	-	-	-	-
Reagents	2 available	4 available	-	-	-	-
Results	3 available	-	-	-	2 available	-
2: LPXN »	Human	Mouse	Rat	Chicken	Fly	Worm
CMKB	LPXN	Lpxn	Lpxn	LPXN	-	-
Entrez Gene	9404	107321	293783	423129	-	-
Uniprot	LPXN_HUMAN	LPXN_MOUSE	-	-	-	-
OMIM	605390	-	-	-	-	-
Reagents	1 available	-	-	-	-	-
Results	-	-	-	-	-	-

Family Summary

Paxillin is a multi-domain protein that localizes to focal adhesions. The C-terminal region of paxillin contains four LIM domains, which target paxillin to focal adhesions, presumably through a direct association with the cytoplasmic tail of beta-integrin. The N-terminal region of paxillin is rich in protein-protein interaction sites. The proteins that bind to paxillin are diverse and include protein tyrosine kinases, such as Src and FAK, structural proteins, such as vinculin and actopaxin, and regulators of actin organization, such as COOL/PIX and PKL/GIT. Paxillin is tyrosine-phosphorylated by FAK and Src upon integrin engagement or growth factor stimulation, creating binding sites for the adapter protein Crk. Leupaxin is preferentially expressed in hematopoietic cells and is homologous to paxillin. It may function in cell type-specific signaling by associating with PYK2, a member of focal adhesion kinase family. As a substrate for a tyrosine kinase in lymphoid cells, this protein may also function in, and be regulated by tyrosine kinase activity.

References

1. Chen PW, Kroog GS. Leupaxin is similar to paxillin in focal adhesion targeting and tyrosine phosphorylation but has distinct roles in cell adhesion and spreading. Cell Adh Migr 2010; 4: (PubMed)
2. Deakin NO, Turner CE. Paxillin comes of age. J. Cell. Sci. 2008; 121:2435-44 (PubMed)
3. Hoefen RJ, Berk BC. The multifunctional GIT family of proteins. J. Cell. Sci. 2006; 119:1469-75 (PubMed)
4. Huang C, Jacobson K, Schaller MD. A role for JNK-paxillin signaling in cell migration. Cell Cycle 2004; 3:4-6 (PubMed)
5. Rathore VB, Okada M, Newman PJ, Newman DK. Paxillin family members function as Csk-binding proteins that regulate Lyn activity in human and murine platelets. Biochem. J. 2007; 403:275-81 (PubMed)
6. Rose DM. The role of the alpha4 integrin-paxillin interaction in regulating leukocyte trafficking. Exp. Mol. Med. 2006; 38:191-5 (PubMed)
7. Sabe H, Onodera Y, Mazaki Y, Hashimoto S. ArfGAP family proteins in cell adhesion, migration and tumor invasion. Curr. Opin. Cell Biol. 2006; 18:558-64 (PubMed)
8. Schaller MD. FAK and paxillin: regulators of N-cadherin adhesion and inhibitors of cell migration?. J. Cell Biol. 2004; 166:157-9 (PubMed)
9. Spinardi L, Marchisio PC. Podosomes as smart regulators of cellular adhesion. Eur. J. Cell Biol. 2006; 85:191-4 (PubMed)
10. Webb DJ, Donais K, Whitmore LA, Thomas SM, Turner CE, Parsons JT, Horwitz AF. FAK-Src signalling through paxillin, ERK and MLCK regulates adhesion disassembly. Nat. Cell Biol. 2004; 6:154-61 (PubMed)

Consortium Results & Data

Consortium Related Products*

^* The resources presented here are largely those generated by the Consortium. The sidebar provides public databases that complement Consortium activities. For mice and biosensors, a public database is not available and therefore we have attempted to generate a migration related list for your convenience.