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  1. Article: Molecular mechanisms of mechanosensing in muscle development.

    Jani, Klodiana / Schöck, Frieder

    Developmental dynamics : an official publication of the American Association of Anatomists

    2009  Volume 238, Issue 6, Page(s) 1526–1534

    Abstract: Mechanical forces are crucial to muscle development and function, but the mechanisms by which forces are sensed and transduced remain elusive. Evidence implicates the sarcolemmal lattice of integrin adhesion and the Z-disk components of the contractile ... ...

    Abstract Mechanical forces are crucial to muscle development and function, but the mechanisms by which forces are sensed and transduced remain elusive. Evidence implicates the sarcolemmal lattice of integrin adhesion and the Z-disk components of the contractile machinery in such processes. These mechanosensory devices report changes in force to other cellular compartments by self-remodeling. Here we explore how their structural and functional properties integrate to regulate muscle development and maintenance. Developmental Dynamics 238:1526-1534, 2009. (c) 2009 Wiley-Liss, Inc.
    MeSH term(s) Animals ; Mechanotransduction, Cellular/physiology ; Muscle Development/physiology ; Muscle Proteins/metabolism ; Muscles/cytology ; Muscles/physiology ; Sarcolemma/metabolism ; Sarcolemma/ultrastructure ; Signal Transduction/physiology
    Chemical Substances Muscle Proteins
    Language English
    Publishing date 2009-06
    Publishing country United States
    Document type Journal Article ; Review
    ZDB-ID 1102541-4
    ISSN 1097-0177 ; 1058-8388
    ISSN (online) 1097-0177
    ISSN 1058-8388
    DOI 10.1002/dvdy.21972
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Zasp is required for the assembly of functional integrin adhesion sites.

    Jani, Klodiana / Schöck, Frieder

    The Journal of cell biology

    2007  Volume 179, Issue 7, Page(s) 1583–1597

    Abstract: The integrin family of heterodimeric transmembrane receptors mediates cell-matrix adhesion. Integrins often localize in highly organized structures, such as focal adhesions in tissue culture and myotendinous junctions in muscles. Our RNA interference ... ...

    Abstract The integrin family of heterodimeric transmembrane receptors mediates cell-matrix adhesion. Integrins often localize in highly organized structures, such as focal adhesions in tissue culture and myotendinous junctions in muscles. Our RNA interference screen for genes that prevent integrin-dependent cell spreading identifies Z band alternatively spliced PDZ-motif protein (zasp), encoding the only known Drosophila melanogaster Alp/Enigma PDZ-LIM domain protein. Zasp localizes to integrin adhesion sites and its depletion disrupts integrin adhesion sites. In tissues, Zasp colocalizes with betaPS integrin in myotendinous junctions and with alpha-actinin in muscle Z lines. Zasp also physically interacts with alpha-actinin. Fly larvae lacking Zasp do not form Z lines and fail to recruit alpha-actinin to the Z line. At the myotendinous junction, muscles detach in zasp mutants with the onset of contractility. Finally, Zasp interacts genetically with integrins, showing that it regulates integrin function. Our observations point to an important function for Zasp in the assembly of integrin adhesion sites both in cell culture and in tissues.
    MeSH term(s) Adaptor Proteins, Signal Transducing/genetics ; Adaptor Proteins, Signal Transducing/metabolism ; Animals ; Carrier Proteins/genetics ; Carrier Proteins/metabolism ; Cell Adhesion/physiology ; Cell Differentiation/genetics ; Cell Line ; Drosophila Proteins/genetics ; Drosophila Proteins/metabolism ; Drosophila melanogaster ; Gene Expression Regulation, Developmental/genetics ; Genetic Testing ; Integrins/metabolism ; LIM Domain Proteins ; Larva ; Muscle, Striated/embryology ; Muscle, Striated/metabolism ; Muscle, Striated/ultrastructure ; Mutation/genetics ; RNA Interference ; Tendons/embryology ; Tendons/metabolism ; Tendons/ultrastructure
    Chemical Substances Adaptor Proteins, Signal Transducing ; Carrier Proteins ; Drosophila Proteins ; Integrins ; LDB3 protein, human ; LIM Domain Proteins ; Zasp52 protein, Drosophila
    Language English
    Publishing date 2007-11-28
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 218154-x
    ISSN 1540-8140 ; 0021-9525
    ISSN (online) 1540-8140
    ISSN 0021-9525
    DOI 10.1083/jcb.200707045
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article: Zasp is required for the assembly of functional integrin adhesion sites

    Jani, Klodiana / Schöck, Frieder

    Journal of cell biology. 2007 Dec. 31, v. 179, no. 7

    2007  

    Abstract: The integrin family of heterodimeric transmembrane receptors mediates cell-matrix adhesion. Integrins often localize in highly organized structures, such as focal adhesions in tissue culture and myotendinous junctions in muscles. Our RNA interference ... ...

    Abstract The integrin family of heterodimeric transmembrane receptors mediates cell-matrix adhesion. Integrins often localize in highly organized structures, such as focal adhesions in tissue culture and myotendinous junctions in muscles. Our RNA interference screen for genes that prevent integrin-dependent cell spreading identifies Z band alternatively spliced PDZ-motif protein (zasp), encoding the only known Drosophila melanogaster Alp/Enigma PDZ-LIM domain protein. Zasp localizes to integrin adhesion sites and its depletion disrupts integrin adhesion sites. In tissues, Zasp colocalizes with βPS integrin in myotendinous junctions and with α-actinin in muscle Z lines. Zasp also physically interacts with α-actinin. Fly larvae lacking Zasp do not form Z lines and fail to recruit α-actinin to the Z line. At the myotendinous junction, muscles detach in zasp mutants with the onset of contractility. Finally, Zasp interacts genetically with integrins, showing that it regulates integrin function. Our observations point to an important function for Zasp in the assembly of integrin adhesion sites both in cell culture and in tissues.
    Language English
    Dates of publication 2007-1231
    Size p. 1583-1597.
    Publishing place The Rockefeller University Press
    Document type Article
    ZDB-ID 218154-x
    ISSN 1540-8140 ; 0021-9525
    ISSN (online) 1540-8140
    ISSN 0021-9525
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  4. Article ; Online: Muscle type-specific expression of Zasp52 isoforms in Drosophila.

    Katzemich, Anja / Long, Jenny Yanyan / Jani, Klodiana / Lee, Byeo Ri / Schöck, Frieder

    Gene expression patterns : GEP

    2011  Volume 11, Issue 8, Page(s) 484–490

    Abstract: Zasp52 is a member of the PDZ-LIM domain protein family in Drosophila, which comprises Enigma, ENH, ZASP, Alp, CLP36, RIL, and Mystique in vertebrates. Drosophila Zasp52 colocalizes with integrins at myotendinous junctions and with α-actinin at Z-disks, ... ...

    Abstract Zasp52 is a member of the PDZ-LIM domain protein family in Drosophila, which comprises Enigma, ENH, ZASP, Alp, CLP36, RIL, and Mystique in vertebrates. Drosophila Zasp52 colocalizes with integrins at myotendinous junctions and with α-actinin at Z-disks, and is required for muscle attachment as well as Z-disk assembly and maintenance. Here we document 13 Zasp52 splice variants giving rise to six different LIM domains. We demonstrate stage- and tissue-specific expression in different muscle types for Zasp52 isoforms encoding different LIM domains. In particular, LIM1b is expressed only in heart muscle and certain somatic muscles, implying muscle-specific functions in Z-disk assembly or maintenance.
    MeSH term(s) Actinin/biosynthesis ; Animals ; Drosophila Proteins/biosynthesis ; Drosophila melanogaster ; Gene Expression Regulation/physiology ; LIM Domain Proteins/biosynthesis ; Muscle Proteins/biosynthesis ; Muscles/metabolism ; Organ Specificity/physiology
    Chemical Substances Drosophila Proteins ; LIM Domain Proteins ; Muscle Proteins ; Zasp52 protein, Drosophila ; Actinin (11003-00-2)
    Language English
    Publishing date 2011-08-17
    Publishing country Netherlands
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2058346-1
    ISSN 1872-7298 ; 1567-133X
    ISSN (online) 1872-7298
    ISSN 1567-133X
    DOI 10.1016/j.gep.2011.08.004
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article: Muscle type-specific expression of Zasp52 isoforms in Drosophila

    Katzemich, Anja / Long, Jenny Yanyan / Jani, Klodiana / Lee, Byeo Ri / Schöck, Frieder

    Gene expression patterns. 2011 Dec., v. 11, no. 8

    2011  

    Abstract: Zasp52 is a member of the PDZ-LIM domain protein family in Drosophila, which comprises Enigma, ENH, ZASP, Alp, CLP36, RIL, and Mystique in vertebrates. Drosophila Zasp52 colocalizes with integrins at myotendinous junctions and with α-actinin at Z-disks, ... ...

    Abstract Zasp52 is a member of the PDZ-LIM domain protein family in Drosophila, which comprises Enigma, ENH, ZASP, Alp, CLP36, RIL, and Mystique in vertebrates. Drosophila Zasp52 colocalizes with integrins at myotendinous junctions and with α-actinin at Z-disks, and is required for muscle attachment as well as Z-disk assembly and maintenance. Here we document 13 Zasp52 splice variants giving rise to six different LIM domains. We demonstrate stage- and tissue-specific expression in different muscle types for Zasp52 isoforms encoding different LIM domains. In particular, LIM1b is expressed only in heart muscle and certain somatic muscles, implying muscle-specific functions in Z-disk assembly or maintenance.
    Keywords Drosophila ; heart ; integrins ; muscles ; vertebrates
    Language English
    Dates of publication 2011-12
    Size p. 484-490.
    Publishing place Elsevier B.V.
    Document type Article
    ZDB-ID 2058346-1
    ISSN 1872-7298 ; 1567-133X
    ISSN (online) 1872-7298
    ISSN 1567-133X
    DOI 10.1016/j.gep.2011.08.004
    Database NAL-Catalogue (AGRICOLA)

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  6. Article ; Online: Zasp regulates integrin activation.

    Bouaouina, Mohamed / Jani, Klodiana / Long, Jenny Y / Czerniecki, Stefan / Morse, Elizabeth M / Ellis, Stephanie J / Tanentzapf, Guy / Schöck, Frieder / Calderwood, David A

    Journal of cell science

    2012  Volume 125, Issue Pt 23, Page(s) 5647–5657

    Abstract: Integrins are heterodimeric adhesion receptors that link the extracellular matrix (ECM) to the cytoskeleton. Binding of the scaffold protein, talin, to the cytoplasmic tail of β-integrin causes a conformational change of the extracellular domains of the ... ...

    Abstract Integrins are heterodimeric adhesion receptors that link the extracellular matrix (ECM) to the cytoskeleton. Binding of the scaffold protein, talin, to the cytoplasmic tail of β-integrin causes a conformational change of the extracellular domains of the integrin heterodimer, thus allowing high-affinity binding of ECM ligands. This essential process is called integrin activation. Here we report that the Z-band alternatively spliced PDZ-motif-containing protein (Zasp) cooperates with talin to activate α5β1 integrins in mammalian tissue culture and αPS2βPS integrins in Drosophila. Zasp is a PDZ-LIM-domain-containing protein mutated in human cardiomyopathies previously thought to function primarily in assembly and maintenance of the muscle contractile machinery. Notably, Zasp is the first protein shown to co-activate α5β1 integrins with talin and appears to do so in a manner distinct from known αIIbβ3 integrin co-activators.
    MeSH term(s) Animals ; Carrier Proteins/metabolism ; Drosophila ; Drosophila Proteins/metabolism ; Extracellular Matrix/metabolism ; Humans ; Integrin alpha5beta1/metabolism ; Integrins/metabolism ; Muscle, Skeletal/metabolism ; Myocardium/metabolism ; Talin/metabolism
    Chemical Substances Carrier Proteins ; Drosophila Proteins ; Integrin alpha5beta1 ; Integrins ; Talin ; Zasp52 protein, Drosophila
    Language English
    Publishing date 2012-09-19
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 2993-2
    ISSN 1477-9137 ; 0021-9533
    ISSN (online) 1477-9137
    ISSN 0021-9533
    DOI 10.1242/jcs.103291
    Database MEDical Literature Analysis and Retrieval System OnLINE

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