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Paxillin is a focal adhesion adapter protein that facilitates the assembly of multiprotein complexes that mediate signal transduction between the extracellular matrix and actin cytoskeleton.1,2,3 It contains four LIM domains in the C-terminal region that target paxillin to focal adhesions and an N-terminal region with five LD motifs that serve as docking sites for a variety of proteins, including vinculin, focal adhesion kinase (FAK), and Src, that facilitate intracellular signal transduction.3 Alternative splicing of PXN generates three isoforms, α, β, and γ, that contain a variable N-terminus, as well as a fourth isoform, δ, that lacks the N-terminal region.3 Paxillin is expressed in most tissues and predominately localizes to focal adhesions on the cell membrane.2,3 Upon cytokine or growth factor stimulation or cell adhesion, paxillin is phosphorylated by a variety of kinases, including FAK and ERK, providing a scaffold for signaling proteins that are involved in the formation and regulation of focal adhesions, which mediate cell migration.3 It is also expressed in the cytoplasm and nucleus where it regulates gene transcription. Tumor paxillin levels are increased in patients with glioblastoma multiforme (GBM) and associated with poor survival. Cayman’s Paxillinα/β/γ (N-Term) Rabbit Monoclonal Antibody (Clone RM256) can be used for immunocytochemistry (ICC) and Western blot (WB) applications.
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1. Paxillin actions in the nucleus. Steroids 133, 87-92 (2018).
2. FAK and paxillin, two potential targets in pancreatic cancer. Oncotarget 7(21), 31586-31601 (2016).
3. Paxillin: A crossroad in pathological cell migration. J. Hematol. Oncol. 10(1), 50 (2017).