Abstract
MARCKS is an actin-modulating protein that can be phosphorylated in multiple sites by PKC and proline-directed kinases. We have previously described a phosphorylated form of this protein specific for differentiating chick neurons, detected with mAb 3C3. Here, we show that this antibody binds to MARCKS only when it is phosphorylated at Ser 25. These and previous data provide hints for a possible answer to the question of why this ubiquitous protein seems to be essential only for neural development.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Antibodies, Monoclonal
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Binding Sites
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Brain / cytology
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Brain / embryology
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Cell Differentiation
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Chick Embryo
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Intracellular Signaling Peptides and Proteins*
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Lipoproteins / chemistry*
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Lipoproteins / metabolism
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Lipoproteins / physiology
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Mass Spectrometry / methods*
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Membrane Proteins / chemistry*
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Membrane Proteins / metabolism
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Membrane Proteins / physiology
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Myristoylated Alanine-Rich C Kinase Substrate
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Neurons / chemistry
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Neurons / cytology
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Phosphoproteins
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Phosphorylation
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Retina / chemistry
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Retina / cytology
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Retina / embryology
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Serine / immunology
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Serine / metabolism
Substances
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Antibodies, Monoclonal
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Intracellular Signaling Peptides and Proteins
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Lipoproteins
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Membrane Proteins
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Phosphoproteins
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Myristoylated Alanine-Rich C Kinase Substrate
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Serine