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pubmed-article:9837946pubmed:abstractTextMacMARCKS (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.lld:pubmed
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pubmed-article:9837946pubmed:dateRevised2007-11-14lld:pubmed
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pubmed-article:9837946pubmed:articleTitleMacMARCKS is not essential for phagocytosis in macrophages.lld:pubmed
pubmed-article:9837946pubmed:affiliationDepartment of Immunology, University of Washington, H-574 Health Sciences, Seattle, Washington 98195, USA.lld:pubmed
pubmed-article:9837946pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:9837946pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
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