MacMARCKS Is Not Essential for Phagocytosis in Macrophages*


MacMARCKS (also known as myristoylated alanine-rich protein kinase C substrate (MARCKS)-related protein) is a member of the MARCKS family of protein kinase C substrates. MacMARCKS contains within it a basic effector domain that contains the serine residues that are phosphorylated by protein kinase C, as well as a calcium/calmodulin and actin-binding site. Two previous reports demonstrated that a macrophage cell line expressing a mutant form of MacMARCKS that lacks the effector domain is defective in phagocytosis and cell adhesion (Zhu, Z., Bao, Z., and Li, J. (1995) J. Biol. Chem. 270, 17652–17655; Li, J., Zhu, Z., and Bao, Z. (1996) J. Biol. Chem. 271, 12985–12990). We report here that macrophages from MacMARCKS null mice phagocytose and spread normally. Thus, although MacMARCKS is recruited to phagosomes, it is not absolutely required for phagocytosis.


  • * This work was supported by Grants AI25032 and AI32972 from the National Institutes of Health.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked “advertisement” in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

  • § Irvington Institute Postdoctoral Fellow.

  • ** To whom correspondence should be addressed: Dept. of Immunology, University of Washington, H-574 Health Sciences, Box 357650, Seattle, WA 98195. Tel.: 206-616-5045; Fax: 206-616-7237; E-mail:aaderem{at}

  • Abbreviations:
    myristoylated alanine-rich protein kinase C substrate
    protein kinase C
    phosphate-buffered saline
    fluorescein isothiocyanate
    • Received August 28, 1998.
    • Revision received September 24, 1998.
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