PUBLICATION
BMP2K phosphorylates AP-2 and regulates clathrin-mediated endocytosis
- Authors
- Ramesh, S.T., Navyasree, K.V., Sah, S., Ashok, A.B., Qathoon, N., Mohanty, S., Swain, R.K., Umasankar, P.K.
- ID
- ZDB-PUB-210905-4
- Date
- 2021
- Source
- Traffic (Copenhagen, Denmark) 22(11): 377-396 (Journal)
- Registered Authors
- Keywords
- none
- MeSH Terms
-
- Adaptor Protein Complex 2*/metabolism
- Animals
- Clathrin*/metabolism
- Endocytosis/physiology
- Phosphorylation
- Zebrafish/metabolism
- PubMed
- 34480404 Full text @ Traffic
Citation
Ramesh, S.T., Navyasree, K.V., Sah, S., Ashok, A.B., Qathoon, N., Mohanty, S., Swain, R.K., Umasankar, P.K. (2021) BMP2K phosphorylates AP-2 and regulates clathrin-mediated endocytosis. Traffic (Copenhagen, Denmark). 22(11):377-396.
Abstract
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. This article is protected by copyright. All rights reserved.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping