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J. Biol. Chem., Vol. 279, Issue 43, 44924-44930, October 22, 2004

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Association of BAP31 with CD11b/CD18

POTENTIAL ROLE IN INTRACELLULAR TRAFFICKING OF CD11b/CD18 IN NEUTROPHILS^*

Ke Zen, Markus Utech¶||, Yuan Liu, Illena Soto, Asma Nusrat, and Charles A. Parkos

From the Epithelial Pathobiology Research Unit, Department of Pathology and Laboratory Medicine, Emory University, Atlanta, Georgia 30322 and ^¶Department of General Surgery, University of Münster, 48149 Münster, Germany

The ₂ integrin CD11b/CD18 is an integral membrane protein that is present in the plasma membrane and secondary granules of neutrophils and functions as a major adhesion molecule. Upon cellular activation, there is translocation of intracellular pools of CD11b/CD18 to the plasma membrane in concert with enhanced cellular adhesion. Although much is known about the function of CD11b/CD18, how this protein is transported within the cell is less well defined. Here we report that CD11b/CD18 specifically binds to BAP31, a member of a novel class of sorting proteins regulating cellular anterograde transport. Through experiments aimed at identifying CD11b/CD18-binding proteins, we produced a monoclonal antibody termed E1B2 that recognizes a 28-kDa membrane protein that co-precipitates with CD11b/CD18. Microsequence analysis of the E1B2 antigen revealed that it is BAP31. Co-association of CD11b/CD18 and BAP31 was confirmed in co-immunoprecipitation and protein binding assays. Additional experiments revealed that the binding of BAP31 to CD11b/CD18 was not dependent on divalent cations nor mediated by the I-domain of CD11b. Using glutathione S-transferase fusion chimeras, we determined that binding of CD11b/CD18 to BAP31 is mediated through interactions with the cytoplasmic tail of BAP31. Immunolocalization studies revealed colocalization of BAP31 and CD11b/CD18 within neutrophil secondary granules. Subcellular fractionation studies in polymorphonuclear leukocytes (PMN) revealed similar patterns of redistribution of BAP31 and CD11b/CD18 from fractions enriched in secondary granules to the plasma membrane following stimulation with formylmethionylleucylphenylalanine (fMLP). Given the known sorting properties of BAP31, these findings suggest that BAP31 may play a role in regulating intracellular trafficking of CD11b/CD18 in neutrophils.

Received for publication, February 25, 2004 , and in revised form, July 26, 2004.

^* This work was supported by Grants HL54229 and HL72124 from the National Institutes of Health (to C. A. P.). Tissue culture and monoclonal antibody production were supported by Digestive Diseases Mini-center Grant DK277640 from the NIDDK, National Institutes of Health. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

^|| Supported by Grant UT 42/1-1 from the German Research Foundation (Deutsche Forschungsgemeinschaft).

To whom correspondence should be addressed: Dept. of Pathology and Laboratory Medicine, Emory University, Whitehead Biomedical Bldg., Rm. 115, 615 Michael St., Atlanta, GA 30322. Tel.: 404-727-8541; Fax: 404-727-3321; E-mail: kzen{at}emory.edu.

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