Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 291, Issue 41, Pages 21335-21349Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M116.742163
Keywords
cell adhesion; cell surface; crystal structure; protein phosphatase; retina; contactin; immunoglobulin|L-like domain
Categories
Funding
- United States Department of Energy, Office of Science, Office of Basic Energy Sciences [W-31-109-Eng-38]
- United States Department of Energy Program Integrated Diffraction Analysis Technologies (IDAT)
- National Institutes of Health [MINOS GM105404]
- NIGMS, National Institutes of Health [P41-GM103311]
Ask authors/readers for more resources
Protein-tyrosine phosphatase receptor type G (RPTP/PTPRG) interacts in vitro with contactin-3-6 (CNTN3-6), a group of glycophosphatidylinositol-anchored cell adhesion molecules involved in the wiring of the nervous system. In addition to PTPRG, CNTNs associate with multiple transmembrane proteins and signal inside the cell via cis-binding partners to alleviate the absence of an intracellular region. Here, we use comprehensive biochemical and structural analyses to demonstrate that PTPRGCNTN3-6 complexes share similar binding affinities and a conserved arrangement. Furthermore, as a first step to identifying PTPRGCNTN complexes in vivo, we found that PTPRG and CNTN3 associate in the outer segments of mouse rod photoreceptor cells. In particular, PTPRG and CNTN3 form cis-complexes at the surface of photoreceptors yet interact in trans when expressed on the surfaces of apposing cells. Further structural analyses suggest that all CNTN ectodomains adopt a bent conformation and might lie parallel to the cell surface to accommodate these cis and trans binding modes. Taken together, these studies identify a PTPRGCNTN complex in vivo and provide novel insights into PTPRG- and CNTN-mediated signaling.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available