Serine phosphorylation of the small phosphoprotein ICAP1 inhibits its nuclear accumulation
Year: 2020
Type: article
Abstract: and in cultured cells and that active PAK4 inhibits ICAP1 nuclear accumulation in a Ser-10-dependent manner. Finally, we show that ICAP1 phosphorylation controls nuclear localization of the ICAP1-KRIT1 complex. We conclude that serine phosphorylation within the ICAP1 N-terminal region can prevent nuclear ICAP1 accumulation, providing a mechanism that regulates KRIT1 localization and signaling, potentially influencing vascular development.
Source: Journal of Biological Chemistry
Institution: Yale University
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: hybrid
Estimated APC paid: $3,430
Awards: Investigation of the role of DNA-binding to the cerebral cavernous malformations protein KRIT1, Institutional National Research Service Award, G5076536658, Phosphorylation of ICAP1 inhibits its nuclear accumulation to modulate integrin and CCM signaling, Molecular assembly and regulation of the cerebral cavernous malformation complex
OpenAlex ID: W3003241878
