Paxillin

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Not to be confused with the neurotoxin paxilline.
Paxillin
Protein PXN PDB 1KKY.png
Rendering based on PDB 1KKY.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols PXN ; FLJ16691
External IDs OMIM602505 MGI108295 HomoloGene37697 ChEMBL: 5715 GeneCards: PXN Gene
Orthologs
Species Human Mouse
Entrez 5829 19303
Ensembl ENSG00000089159 ENSMUSG00000029528
UniProt P49023 Q8VI36
RefSeq (mRNA) NM_001080855 NM_011223
RefSeq (protein) NP_001074324 NP_035353
Location (UCSC) Chr 12:
120.65 – 120.7 Mb
Chr 5:
115.51 – 115.56 Mb
PubMed search [1] [2]

Paxillin is a signal transduction adaptor protein discovered in 1990 in the laboratory of Keith Burridge.[1] The C-terminal region of paxillin contains four LIM domains that target paxillin to focal adhesions. It is presumed 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 focal adhesion kinase (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.[2]


References[edit]

  1. ^ Turner, C. E., Glenney, J. R., Jr. & Burridge, K. Paxillin: a new vinculin-binding protein present in focal adhesions. J Cell Biol 111, 1059–1068 (1990).
  2. ^ From the Cell Migration Knowledgebase

Further reading[edit]

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