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Full-Text Articles in Medicine and Health Sciences
A Single Base Pair Mutation Encoding A Premature Stop Codon In The Mis Type Ii Receptor Is Responsible For Canine Persistent Mullerian Duct Syndrome, Wenfang Wu, Shengqin Wan, Pujar Shashikant, Mark Haskins, Donald Schlafer, Mary Lee, Vicki Meyers-Wallen
A Single Base Pair Mutation Encoding A Premature Stop Codon In The Mis Type Ii Receptor Is Responsible For Canine Persistent Mullerian Duct Syndrome, Wenfang Wu, Shengqin Wan, Pujar Shashikant, Mark Haskins, Donald Schlafer, Mary Lee, Vicki Meyers-Wallen
Mary M. Lee
Mullerian inhibiting substance (MIS), a secreted glycoprotein in the transforming growth factor-beta family of growth factors, mediates regression of the Mullerian ducts during embryonic sex differentiation in males. In persistent Mullerian duct syndrome (PMDS), rather than undergoing involution, the Mullerian ducts persist in males, giving rise to the uterus, fallopian tubes, and upper vagina. Genetic defects in MIS or its receptor (MISRII) have been identified in patients with PMDS. The phenotype in the canine model of PMDS derived from the miniature schnauzer breed is strikingly similar to that of human patients. In this model, PMDS is inherited as a sex-limited …
Evidence That Distinct States Of The Integrin Alpha6beta1 Interact With Laminin And An Adam, M. S. Chen, E. A. Almeida, A. P. Huovila, Y. Takahashi, Leslie M. Shaw, Arthur M. Mercurio, J. M. White
Evidence That Distinct States Of The Integrin Alpha6beta1 Interact With Laminin And An Adam, M. S. Chen, E. A. Almeida, A. P. Huovila, Y. Takahashi, Leslie M. Shaw, Arthur M. Mercurio, J. M. White
Arthur M. Mercurio
Integrins can exist in different functional states with low or high binding capacity for particular ligands. We previously provided evidence that the integrin alpha6beta1, on mouse eggs and on alpha6-transfected cells, interacted with the disintegrin domain of the sperm surface protein ADAM 2 (fertilin beta). In the present study we tested the hypothesis that different states of alpha6beta1 interact with fertilin and laminin, an extracellular matrix ligand for alpha6beta1. Using alpha6-transfected cells we found that treatments (e.g., with phorbol myristate acetate or MnCl2) that increased adhesion to laminin inhibited sperm binding. Conversely, treatments that inhibited laminin adhesion increased sperm binding. …
Regulation Of Alpha 6 Beta 1 Integrin Laminin Receptor Function By The Cytoplasmic Domain Of The Alpha 6 Subunit, Leslie M. Shaw, Arthur M. Mercurio
Regulation Of Alpha 6 Beta 1 Integrin Laminin Receptor Function By The Cytoplasmic Domain Of The Alpha 6 Subunit, Leslie M. Shaw, Arthur M. Mercurio
Arthur M. Mercurio
The alpha 6 beta 1 integrin is expressed on the macrophage surface in an inactive state and requires cellular activation with PMA or cytokines to function as a laminin receptor (Shaw, L. M., J. M. Messier, and A. M. Mercurio. 1990. J. Cell Biol. 110:2167-2174). In the present study, the role of the alpha 6 subunit cytoplasmic domain in alpha 6 beta 1 integrin activation was examined. The use of P388D1 cells, an alpha 6-integrin deficient macrophage cell line, facilitated this analysis because expression of either the alpha 6A or alpha 6B subunit cDNAs restores their activation responsive laminin adhesion …
Patellin1, A Novel Sec14-Like Protein, Localizes To The Cell Plate And Binds Phosphoinositides, T. Peterman, Yamini Ohol, Lisa Mcreynolds, Elizabeth Luna
Patellin1, A Novel Sec14-Like Protein, Localizes To The Cell Plate And Binds Phosphoinositides, T. Peterman, Yamini Ohol, Lisa Mcreynolds, Elizabeth Luna
Elizabeth J. Luna
Membrane trafficking is central to construction of the cell plate during plant cytokinesis. Consequently, a detailed understanding of the process depends on the characterization of molecules that function in the formation, transport, targeting, and fusion of membrane vesicles to the developing plate, as well as those that participate in its consolidation and maturation into a fully functional partition. Here we report the initial biochemical and functional characterization of patellin1 (PATL1), a novel cell-plate-associated protein that is related in sequence to proteins involved in membrane trafficking in other eukaryotes. Analysis of the Arabidopsis genome indicated that PATL1 is one of a …
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
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 …
Merlin Differs From Moesin In Binding To F-Actin And In Its Intra- And Intermolecular Interactions, L. Huang, E. Ichimaru, Kersi Pestonjamasp, X. Cui, H. Nakamura, G. Lo, F. Lin, Elizabeth Luna, H. Furthmayr
Merlin Differs From Moesin In Binding To F-Actin And In Its Intra- And Intermolecular Interactions, L. Huang, E. Ichimaru, Kersi Pestonjamasp, X. Cui, H. Nakamura, G. Lo, F. Lin, Elizabeth Luna, H. Furthmayr
Elizabeth J. Luna
The neurofibromatosis type 2 (NF2) tumor suppressor gene encodes merlin, a protein with homology to the cell membrane/F-actin linking proteins, moesin, ezrin and radixin. Unlike these closely related proteins, merlin lacks a C-terminal F-actin binding site detectable by actin blot overlays, and the GFP-tagged merlin C-terminal domain co-distributes with neither stress fibers nor cortical actin in NIH3T3 cells. Merlin also differs from the other three proteins in its inter- and intramolecular domain interactions, as shown by in vitro binding and yeast two-hybrid assays. As is true for ezrin, moesin and radixin, the N- and C-terminal domains of merlin type 1 …
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
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 …
F-Actin And Myosin Ii Binding Domains In Supervillin, Yu Chen, Norio Takizawa, Jessica Crowley, Sang Oh, Cheryl Gatto, Taketoshi Kambara, Osamu Sato, Xiang-Dong Li, Mitsuo Ikebe, Elizabeth Luna
F-Actin And Myosin Ii Binding Domains In Supervillin, Yu Chen, Norio Takizawa, Jessica Crowley, Sang Oh, Cheryl Gatto, Taketoshi Kambara, Osamu Sato, Xiang-Dong Li, Mitsuo Ikebe, Elizabeth Luna
Elizabeth J. Luna
Detergent-resistant membranes contain signaling and integral membrane proteins that organize cholesterol-rich domains called lipid rafts. A subset of these detergent-resistant membranes (DRM-H) exhibits a higher buoyant density ( approximately 1.16 g/ml) because of association with membrane skeleton proteins, including actin, myosin II, myosin 1G, fodrin, and an actin- and membrane-binding protein called supervillin (Nebl, T., Pestonjamasp, K. N., Leszyk, J. D., Crowley, J. L., Oh, S. W., and Luna, E. J. (2002) J. Biol. Chem. 277, 43399-43409). To characterize interactions among DRM-H cytoskeletal proteins, we investigated the binding partners of the novel supervillin N terminus, specifically amino acids 1-830. We …
Archvillin, A Muscle-Specific Isoform Of Supervillin, Is An Early Expressed Component Of The Costameric Membrane Skeleton, Sang W. Oh, Robert K. Pope, Kelly P. Smith, Jessica Lynn Crowley, Thomas Nebl, Jeanne B. Lawrence, Elizabeth J. Luna
Archvillin, A Muscle-Specific Isoform Of Supervillin, Is An Early Expressed Component Of The Costameric Membrane Skeleton, Sang W. Oh, Robert K. Pope, Kelly P. Smith, Jessica Lynn Crowley, Thomas Nebl, Jeanne B. Lawrence, Elizabeth J. Luna
Elizabeth J. Luna
The membrane skeleton protein supervillin binds tightly to both F-actin and membranes and can potentiate androgen receptor activity in non-muscle cells. We report that muscle, which constitutes the principal tissue source for supervillin sequences, contains a approximately 250 kDa isoform of supervillin that localizes within nuclei and with dystrophin at costameres, regions of F-actin membrane attachment in skeletal muscle. The gene encoding this protein, 'archvillin' (Latin, archi; Greek, archos; 'principal' or 'chief'), contains an evolutionarily conserved, muscle-specific 5' leader sequence. Archvillin cDNAs also contain four exons that encode approximately 47 kDa of additional muscle-specific protein sequence in the form of …