MacMARCKS Is Not Essential for Phagocytosis in Macrophages

作者：David M. Underhill, Jianmin Chen, Lee‐Ann H. Allen, Alan A. Aderem · 发表于：Journal of Biological Chemistry · 年份：1998 · DOI：10.1074/jbc.273.50.33619 · 被引用次数：36 · 研究领域：Cellular transport and secretion、Protein Kinase Regulation and GTPase Signaling、Phagocytosis and Immune Regulation

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.