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Definition of Family of Coronin-Related Proteins Conserved Between Humans and Mice: Close Genetic Linkage Between Coronin-2 and CD45-Associated Protein. MEINOSHIN OKUMURA, CHUN KUNG, STEPHANIE WONG, MARTIN RODGERS, MATTHEW L.Journal of Investigative Dermatology 1998, 111 Human Langerhans Cells Express a Novel Form of the Leukocyte Common Antigen (CD45). Journal of Biological Chemistry 1999, 274 Definition of the Sites of Interaction between the Protein Tyrosine Phosphatase SHP-1 and CD22. Julie Blasioli, Silke Paust, Matthew L.Interactions of CD45-associated Protein with the Antigen Receptor Signaling Machinery in T-lymphocytes. André Veillette, David Soussou, Sylvain Latour, Dominique Davidson, François G.CD45-associated protein is not essential for the regulation of antigen receptor-mediated signal transduction. Proceedings of the National Academy of Sciences 2000, 97 A supramolecular basis for CD45 tyrosine phosphatase regulation in sustained T cell activation. Transmembrane homodimerization of receptor-like protein tyrosine phosphatases. Profiling of the CD4 receptor complex proteins. Distinct Transcriptomic Features are Associated with Transitional and Mature B-Cell Populations in the Mouse Spleen. Dykxhoorn, Enrico Capobianco, Akiko Takeda, Jean-Christophe Renauld, Wasif N. Eden Kleiman, Daria Salyakina, Magali De Heusch, Kristen L.Journal of Biological Chemistry 2019, 294 Disrupting the transmembrane domain–mediated oligomerization of protein tyrosine phosphatase receptor J inhibits EGFR-driven cancer cell phenotypes. This article is cited by 12 publications. However, the expression of chimeric transmembrane regions indicates that a minimum of three and a maximum of eight amino acids in this region are sufficient to allow interaction with CD45AP. Alanine-scan mutations of the CD45 transmembrane region demonstrate that no single amino acid is essential for the interaction with CD45AP. To further characterize this interaction, chimeric proteins containing mutations in CD45 transmembrane regions were expressed, and their ability to associate with CD45AP was determined. Therefore, CD45AP is localized to the plasma membrane.
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Cell surface labeling and coimmunoprecipitation demonstrate that CD45AP associates with surface-expressed CD45. Pulse−chase analysis indicates that CD45 associates with CD45AP within minutes of biosynthesis. Cells lines and mice deficient in CD45 express CD45AP mRNA, yet the protein is poorly expressed, indicating that CD45 is required for efficient expression of CD45AP. The lymphoid-specific CD45-associated protein, CD45AP, interacts with CD45 through transmembrane interactions. The inability to activate p56 lck in CD45-deficient cells results in a higher threshold of signaling through the T cell receptor. The transmembrane protein tyrosine phosphatase CD45 functions to activate Src-family member kinase activity in T lymphocytes.