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    Smooth muscle archvillin: a novel regulator of signaling and contractility in vascular smooth muscle

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    Authors
    Gangopadhyay, Samudra S.
    Takizawa, Norio
    Gallant, Cynthia
    Barber, Amy L.
    Je, Hyun-Dong
    Smith, Tara C.
    Luna, Elizabeth J.
    Morgan, Kathleen G.
    UMass Chan Affiliations
    Department of Cell Biology
    Document Type
    Journal Article
    Publication Date
    2004-09-24
    Keywords
    Alternative Splicing
    Amino Acid Sequence
    Animals
    Aorta
    Blotting, Western
    COS Cells
    Calcium-Binding Proteins
    DNA, Complementary
    Enzyme Activation
    Ferrets
    Glutathione Transferase
    Membrane Proteins
    Microfilament Proteins
    Microscopy, Fluorescence
    Mitogen-Activated Protein Kinase 1
    Mitogen-Activated Protein Kinase 3
    Models, Genetic
    Molecular Sequence Data
    Muscle, Smooth
    Oligonucleotides, Antisense
    Phosphorylation
    Protein Binding
    Protein Kinase C
    Protein Structure, Tertiary
    Recombinant Proteins
    Reverse Transcriptase Polymerase Chain Reaction
    Sequence Homology, Amino Acid
    Signal Transduction
    Subcellular Fractions
    Time Factors
    Transfection
    Two-Hybrid System Techniques
    Cell Biology
    Life Sciences
    Medicine and Health Sciences
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    Abstract
    The mechanisms by which protein kinase C (PKC) and extracellular-signal-regulated kinases (ERK1/2) govern smooth-muscle contractility remain unclear. Calponin (CaP), an actin-binding protein and PKC substrate, mediates signaling through ERK1/2. We report here that CaP sequences containing the CaP homology (CH) domain bind to the C-terminal 251 amino acids of smooth-muscle archvillin (SmAV), a new splice variant of supervillin, which is a known actin- and myosin-II-binding protein. The CaP-SmAV interaction is demonstrated by reciprocal yeast two-hybrid and blot-overlay assays and by colocalization in COS-7 cells. In differentiated smooth muscle, endogenous SmAV and CaP co-fractionate and co-translocate to the cell cortex after stimulation by agonist. Antisense knockdown of SmAV in tissue inhibits both the activation of ERK1/2 and contractions stimulated by either agonist or PKC activation. This ERK1/2 signaling and contractile defect is similar to that observed in CaP knockdown experiments. In A7r5 smooth-muscle cells, PKC activation by phorbol esters induces the reorganization of endogenous, membrane-localized SmAV and microfilament-associated CaP into podosome-like structures that also contain F-actin, nonmuscle myosin IIB and ERK1/2. These results indicate that SmAV contributes to the regulation of contractility through a CaP-mediated signaling pathway, involving PKC activation and phosphorylation of ERK1/2.
    Source
    J Cell Sci. 2004 Oct 1;117(Pt 21):5043-57. Epub 2004 Sep 21. Link to article on publisher's site
    DOI
    10.1242/jcs.01378
    Permanent Link to this Item
    http://hdl.handle.net/20.500.14038/50784
    PubMed ID
    15383618
    Related Resources
    Link to article in PubMed
    ae974a485f413a2113503eed53cd6c53
    10.1242/jcs.01378
    Scopus Count
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    UMass Chan Faculty and Researcher Publications
    Radiology Publications
    Luna Lab

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