BMP2K phosphorylates AP-2 and regulates clathrin-mediated endocytosis.

Traffic  03 September 2021| 

Shikha T. Ramesh, Kolaparamba V. Navyasree, Sneha Sah, Anjitha B. Ashok, Nishada Qathoon, Suryasikha Mohanty, Rajeeb K. Swain, Perunthottathu K. Umasankar


Phosphorylation of the central adaptor protein complex, AP-2 is pivotal for clathrin-mediated endocytosis (CME). Here, we uncover the role of an uncharacterized kinase (BMP-2 inducible kinase- BMP2K) in AP-2 phosphorylation. We demonstrate that BMP2K can phosphorylate AP-2 in vitro and in vivo. Functional impairment of BMP2K impedes AP-2 phosphorylation leading to defects in clathrin-coated pit (CCP) morphology and cargo internalization. BMP2K engages AP-2 via its extended C-terminus and this interaction is important for its CCP localization and function. Notably, endogenous BMP2K levels decline upon functional impairment of AP-2 indicating AP-2 dependent BMP2K stabilization in cells. Further, functional inactivation of BMP2K in zebrafish embryos yields gastrulation phenotypes which mirror AP-2 loss-of-function suggesting physiological relevance of BMP2K in vertebrates. Together, our findings propose involvement of a novel kinase in AP-2 phosphorylation and in the operation of CME.


Rajiv Gandhi Centre for Biotechnology (RGCB),
Thycaud Post, Poojappura,
Thiruvananthapuram - 695 014, Kerala, India
+91-471-2529400 | 2347975 | 2348753

My Gov Prime Ministers National Relife Fund India Gov Make In India Make In India Data gov in

Last Updated on: September 23, 2021
CERT-In Certified Website