Work

Cutting Edge: The B Cell Surface Protein CD72 Recruits the Tyrosine Phosphatase SHP-1 upon Tyrosine Phosphorylation

Year: 1998

Type: article

Abstract: Activation signals of lymphocytes are negatively regulated by the membrane molecules carrying the immunoreceptor tyrosine-based inhibition motif (ITIM). Upon tyrosine phosphorylation, ITIMs recruit SH2-containing phosphatases such as SHP-1, resulting in down-modulation of cell activation. We showed that the cytoplasmic domain of the CD72 molecule carries an ITIM and is associated in vitro with SHP-1 upon tyrosine phosphorylation. Moreover, cross-linking of B cell Ag receptor (BCR) enhances both tyrosine phosphorylation of CD72 and association of CD72 with SHP-1 in B cell line WEHI-231. These results indicate that CD72 recruits SHP-1 upon tyrosine phosphorylation induced by BCR signaling, suggesting that CD72 is a negative regulator of BCR signaling.

Source: The Journal of Immunology

DOI: 10.4049/jimmunol.160.10.4662

Authors: Takahiro Adachi, Heinrich Flaswinkel, Hidetaka Yakura, Michael Reth, Takeshi Tsubata

Institutions: Tokyo Medical and Dental University, University of Freiburg

Language: English

Topic: Protein Tyrosine Phosphatases

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: bronze

Funders: Uehara Memorial Foundation, Tokyo Medical and Dental University, Japan Science and Technology Agency, National Institute of Allergy and Infectious Diseases

OpenAlex ID: W4313376294