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Phospholipases: structural and functional motifs for working at an interface
Author(s) -
Roberts Mary F.
Publication year - 1996
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.10.10.8751718
Subject(s) - phospholipase , phosphoinositide phospholipase c , phosphatidylinositol , biochemistry , cytoplasm , pleckstrin homology domain , phospholipase c , chemistry , second messenger system , structural motif , diacylglycerol kinase , ribonuclease , signal transduction , biology , microbiology and biotechnology , enzyme , protein kinase c , gene , rna
Phospholipases form a ubiquitous class of enzymes optimized to catalyze the hydrolysis of phospholipids. Because their products are often second messengers, they are highly regulated by the cell. For a given ester bond, there are separate secreted as well as cytoplasmic phospholipases with different substrate specificities and modes of regulation. As it becomes available, structural information provides a view of interfacial catalysis for several of these phospholipases on a molecular level. Recent structural advances include solution structures of a pancreatic phospholipase A 2 in the absence and presence of a micellar interface, crystal structures of a bacterial phosphatidylinositol‐phospholipase C whose active site is reminiscent of ribonuclease, and a Ca 2+ lipid binding domain with high homology to regions in several cytoplasmic phospholipases that can model the way those proteins interact with the membrane surface. Phospholipases also have a wide and complex array of regulatory mechanisms involving cytoplasmic proteins, notably G‐proteins, as well as different effector lipids (e.g., phosphatidylinositol‐4, 5‐biphosphate, or PIP 2 ) or Ca 2+ . Deconvolution of these interactions is necessary to understand their roles in different signal transduction path‐ways.—Roberts, M. F. Phospholipases: structural and functional motifs for working at an interface. FASEB J. 10, 1159‐1172(1996)