Pseudopodium enriched atypical kinase 1 (PEAK1)

Pseudopodium enriched atypical kinase 1 (PEAK1) is a cytoskeleton-associated, non-receptor tyrosine kinase and scaffolding protein that regulates cell migration, proliferation, and cytoskeletal dynamics[2][3][6][7]. It localizes to actin filaments and focal adhesions, modulating focal adhesion elongation and transmitting signals from integrin and growth factor receptors such as EGFR[2][7]. Although classified as a probable catalytically inactive kinase, PEAK1 acts as a molecular scaffold integrating Src, Crk, Grb2, and other signaling adaptors to regulate communication between the extracellular matrix, cytoskeleton, and intracellular pathways—playing a central role in cancer metastasis, tumorigenesis, and pathological angiogenesis[3][7]. Elevated PEAK1 expression is strongly associated with progression and poor prognosis in multiple cancers, making it a candidate therapeutic target in oncology, particularly where aberrant cytoskeletal dynamics and new vessel formation drive disease[1][3][7].

Other names

PEAK1SGK269Sugen kinase 269Tyrosine-protein kinase SgK269Inactive tyrosine-protein kinase PEAK1KIAA2002Pseudopodium-enriched atypical kinase 1NKF3 kinase family member

Not directly targeted by approved drugs; experimental inhibition via JAK/STAT3 signaling blockade in the context of PEAK1-induced activity[1] Functions as a signaling scaffold integrating cytoskeletal and extracellular matrix signals[7]