The role of small adaptor proteins in the control of oncogenic signalingr driven by tyrosine kinases in human cancer

Oncotarget
Cécile NaudinSerge Roche

Abstract

Protein phosphorylation on tyrosine (Tyr) residues has evolved as an important mechanism to coordinate cell communication in multicellular organisms. The importance of this process has been revealed by the discovery of the prominent oncogenic properties of tyrosine kinases (TK) upon deregulation of their physiological activities, often due to protein overexpression and/or somatic mutation. Recent reports suggest that TK oncogenic signaling is also under the control of small adaptor proteins. These cytosolic proteins lack intrinsic catalytic activity and signal by linking two functional members of a catalytic pathway. While most adaptors display positive regulatory functions, a small group of this family exerts negative regulatory functions by targeting several components of the TK signaling cascade. Here, we review how these less studied adaptor proteins negatively control TK activities and how their loss of function induces abnormal TK signaling, promoting tumor formation. We also discuss the therapeutic consequences of this novel regulatory mechanism in human oncology.

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Citations

Jun 18, 2016·Clinical and Experimental Pharmacology & Physiology·Yinliang QiShuyu Gui
Jul 14, 2020·The Journal of Clinical Investigation·Mary Wines-SamuelsonBradford C Berk
Aug 1, 2020·Scandinavian Journal of Immunology·Paweł BorowiczAnne Spurkland
Sep 2, 2021·Antioxidants & Redox Signaling·Helen WedegaertnerJoann Trejo
Dec 3, 2021·Biological & Pharmaceutical Bulletin·Tadashi Matsuda, Kenji Oritani

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Methods Mentioned

BETA
ubiquitination
myristoylation
two-hybrid
GTPases

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