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Selected Works

Selected Works

2008

Sequence Homology, Amino Acid

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Full-Text Articles in Medicine and Health Sciences

Supervillin (P205): A Novel Membrane-Associated, F-Actin-Binding Protein In The Villin/Gelsolin Superfamily, Kersi N. Pestonjamasp, Robert K. Pope, J. D. Wulfkuhle, Elizabeth J. Luna Mar 2008

Supervillin (P205): A Novel Membrane-Associated, F-Actin-Binding Protein In The Villin/Gelsolin Superfamily, Kersi N. Pestonjamasp, Robert K. Pope, J. D. Wulfkuhle, Elizabeth J. Luna

Elizabeth J. Luna

Actin-binding membrane proteins are involved in both adhesive interactions and motile processes. We report here the purification and initial characterization of p205, a 205-kD protein from bovine neutrophil plasma membranes that binds to the sides of actin filaments in blot overlays. p205 is a tightly bound peripheral membrane protein that cosediments with endogenous actin in sucrose gradients and immunoprecipitates. Amino acid sequences were obtained from SDS-PAGE-purified p205 and used to generate antipeptide antibodies, immunolocalization data, and cDNA sequence information. The intracellular localization of p205 in MDBK cells is a function of cell density and adherence state. In subconfluent cells, p205 …


Smooth Muscle Archvillin: A Novel Regulator Of Signaling And Contractility In Vascular Smooth Muscle, Samudra S. Gangopadhyay, Norio Takizawa, Cynthia Gallant, Amy L. Barber, Hyun-Dong Je, Tara C. Smith, Elizabeth J. Luna, Kathleen G. Morgan Mar 2008

Smooth Muscle Archvillin: A Novel Regulator Of Signaling And Contractility In Vascular Smooth Muscle, Samudra S. Gangopadhyay, Norio Takizawa, Cynthia Gallant, Amy L. Barber, Hyun-Dong Je, Tara C. Smith, Elizabeth J. Luna, Kathleen G. Morgan

Elizabeth J. Luna

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 …