1. Academic Validation
  2. ACAP4 interacts with CrkII to promote the recycling of integrin β1

ACAP4 interacts with CrkII to promote the recycling of integrin β1

  • Biochem Biophys Res Commun. 2019 Aug 13;516(1):8-14. doi: 10.1016/j.bbrc.2019.05.173.
Xueyan Song 1 Wenjuan Xu 1 Guangsheng Xu 1 Shuai Kong 1 Lu Ding 1 Jin Xiao 2 Xinwang Cao 1 Fengsong Wang 3
Affiliations

Affiliations

  • 1 School of Life Sciences, Anhui Medical University, Hefei, 230032, China.
  • 2 Department of Neurosurgery, First Affiliated Hospital of Anhui Medical University, Hefei, 230032, China.
  • 3 School of Life Sciences, Anhui Medical University, Hefei, 230032, China. Electronic address: fengsongw@ahmu.edu.cn.
Abstract

ACAP4, a GTPase-activating protein (GAP) for the ADP-ribosylation factor 6 (ARF6), plays import roles in cell migration, cell polarity, vesicle trafficking and tumorigenesis. Similarly, the ubiquitously expressed adaptor protein CrkII functions in a wide range of cellular activities, including cell proliferation, T cell adhesion and activation, tumorigenesis, and Bacterial pathogenesis. Here, we demonstrate that ACAP4 physically interacts with CrkII. Biochemical experiments revealed that ACAP4550-660 and the SH3N domain of CrkII are responsible for the interaction. Functional characterization showed that the interaction is required for the recruitment of ACAP4 to the plasma membrane where ACAP4 functions to regulate the recycling of the signal transducer Integrin β1. Thus, we suggest that the CrkII-ACAP4 complex may be involved in regulation of cell adhesion.

Keywords

ACAP4; Cell adhesion; CrkII; Integrin β1; Recycling.

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