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Hematopoietic cell phosphatase is recruited to CD22 following B cell antigen receptor ligation.
J Biol Chem. 1995 Sep 01; 270(35):20305-8.JB

Abstract

Hematopoietic cell phosphatase is a nonreceptor protein tyrosine phosphatase that is preferentially expressed in hematopoietic cell lineages. Motheaten mice, which are devoid of (functional) hematopoietic cell phosphatase, have severe disturbances in the regulation of B cell activation and differentiation. Because signals transduced via the B cell antigen receptor are known to guide these processes, we decided to analyze molecular interactions between the hematopoietic cell phosphatase and the B cell antigen receptor. Ligation of the B cell antigen receptor induces moderate tyrosine phosphorylation of hematopoietic cell phosphatase and the formation of a multi-molecular complex containing additional 68-70- and 135-kDa phosphoproteins. In resting B cells most of the hematopoietic cell phosphatase proteins reside in the cytosolic compartment, whereas after B cell antigen receptor cross-linking, a small fraction translocates toward the membrane where it specifically binds to the 135-kDa phosphoprotein. This 135-kDa glycoprotein was identified as CD22, a transmembrane associate of the B cell antigen receptor complex. Together these findings provide the first direct evidence that this cytoplasmic tyrosine phosphatase is involved in antigen receptor-mediated B cell activation, suggesting that in vivo B cell antigen receptor constituents or associated molecules may serve as substrate for its catalytic activity.

Authors+Show Affiliations

Central Laboratory of the Blood Transfusion Service, The Netherlands Red Cross, University of Amsterdam.No affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article

Language

eng

PubMed ID

7657601

Citation

Lankester, A C., et al. "Hematopoietic Cell Phosphatase Is Recruited to CD22 Following B Cell Antigen Receptor Ligation." The Journal of Biological Chemistry, vol. 270, no. 35, 1995, pp. 20305-8.
Lankester AC, van Schijndel GM, van Lier RA. Hematopoietic cell phosphatase is recruited to CD22 following B cell antigen receptor ligation. J Biol Chem. 1995;270(35):20305-8.
Lankester, A. C., van Schijndel, G. M., & van Lier, R. A. (1995). Hematopoietic cell phosphatase is recruited to CD22 following B cell antigen receptor ligation. The Journal of Biological Chemistry, 270(35), 20305-8.
Lankester AC, van Schijndel GM, van Lier RA. Hematopoietic Cell Phosphatase Is Recruited to CD22 Following B Cell Antigen Receptor Ligation. J Biol Chem. 1995 Sep 1;270(35):20305-8. PubMed PMID: 7657601.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Hematopoietic cell phosphatase is recruited to CD22 following B cell antigen receptor ligation. AU - Lankester,A C, AU - van Schijndel,G M, AU - van Lier,R A, PY - 1995/9/1/pubmed PY - 1995/9/1/medline PY - 1995/9/1/entrez SP - 20305 EP - 8 JF - The Journal of biological chemistry JO - J Biol Chem VL - 270 IS - 35 N2 - Hematopoietic cell phosphatase is a nonreceptor protein tyrosine phosphatase that is preferentially expressed in hematopoietic cell lineages. Motheaten mice, which are devoid of (functional) hematopoietic cell phosphatase, have severe disturbances in the regulation of B cell activation and differentiation. Because signals transduced via the B cell antigen receptor are known to guide these processes, we decided to analyze molecular interactions between the hematopoietic cell phosphatase and the B cell antigen receptor. Ligation of the B cell antigen receptor induces moderate tyrosine phosphorylation of hematopoietic cell phosphatase and the formation of a multi-molecular complex containing additional 68-70- and 135-kDa phosphoproteins. In resting B cells most of the hematopoietic cell phosphatase proteins reside in the cytosolic compartment, whereas after B cell antigen receptor cross-linking, a small fraction translocates toward the membrane where it specifically binds to the 135-kDa phosphoprotein. This 135-kDa glycoprotein was identified as CD22, a transmembrane associate of the B cell antigen receptor complex. Together these findings provide the first direct evidence that this cytoplasmic tyrosine phosphatase is involved in antigen receptor-mediated B cell activation, suggesting that in vivo B cell antigen receptor constituents or associated molecules may serve as substrate for its catalytic activity. SN - 0021-9258 UR - https://www.unboundmedicine.com/medline/citation/7657601/Hematopoietic_cell_phosphatase_is_recruited_to_CD22_following_B_cell_antigen_receptor_ligation_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0021-9258(18)90385-6 DB - PRIME DP - Unbound Medicine ER -