Raftlin is recruited by neuropilin-1 to the activated VEGFR2 complex to control proangiogenic signaling.

ABSTRACT:

Background

VEGFR2 (vascular endothelial growth factor receptor 2) is the major pro-angiogenic receptor in endothelial cells. Compared to other members of the receptor tyrosine kinase family, we know relatively few VEGFR2 signaling partners. Our objective was to use mass spectrometry-based proteomics to identify novel binding partners of activated VEGFR2.

Methods

We created an endothelial cell line stably expressing GFP-tagged VEGFR2 and isolated activated receptor complexes. Analysis by mass spectrometry identified raftlin as a novel binding partner of VEGFR2.

Results

We found that raftlin is recruited to the activated VEGFR2 complex via the co-receptor Nrp1 (neuropilin-1). We show that raftlin regulates the surface levels of Nrp1 in endothelial cells, controlling the

SUBMITTER: Bayliss AL 

PROVIDER: S-EPMC7311514 | biostudies-literature | 2020 Aug

REPOSITORIES: biostudies-literature