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Requirements for the localization of nesprin-3 at the nuclear envelope and its interaction with plectin.

Requirements for the localization of nesprin-3 at the nuclear envelope and its interaction with plectin. Research Abstract Details 

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  • Requirements for the localization of nesprin-3 at the nuclear envelope and its interaction with plectin. Abstract Text:

    mirjam ketemaMirjam Ketema,kevin wilhelmsenKevin Wilhelmsen,ingrid kuikmanIngrid Kuikman,hans janssenHans Janssen,didier hodzicDidier Hodzic,arnoud sonnenbergArnoud Sonnenberg,

    The outer nuclear membrane proteins nesprin-1 and nesprin-2 are retained at the nuclear envelope through an interaction of their klarsicht/ANC-1/syne homology (KASH) domain with Sun proteins present at the inner nuclear membrane. We investigated the requirements for the localization of nesprin-3alpha at the outer nuclear membrane and show that the mechanism by which its localization is mediated is similar to that reported for the localization of nesprin-1 and nesprin-2: the last four amino acids of the nesprin-3alpha KASH domain are essential for its interaction with Sun1 and Sun2. Moreover, deletion of these amino acids or knockdown of the Sun proteins results in a redistribution of nesprin-3alpha away from the nuclear envelope and into the endoplasmic reticulum (ER), where it becomes colocalized with the cytoskeletal crosslinker protein plectin. Both nesprin-3alpha and plectin can form dimers, and dimerization of plectin is required for its interaction with nesprin-3alpha at the nuclear envelope, which is mediated by its N-terminal actin-binding domain. Additionally, overexpression of the plectin actin-binding domain stabilizes the actin cytoskeleton and prevents the recruitment of endogenous plectin to the nuclear envelope. Our studies support a model in which the actin cytoskeleton influences the binding of plectin dimers to dimers of nesprin-3alpha, which in turn are retained at the nuclear envelope through an interaction with Sun proteins.

    Requirements for the localization of nesprin-3 at the nuclear envelope and its interaction with plectin. Publishing Authors By Initials

    m ketemaM Ketema,k wilhelmsenK Wilhelmsen,i kuikmanI Kuikman,h janssenH Janssen,d hodzicD Hodzic,a sonnenbergA Sonnenberg,

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    Requirements for the localization of nesprin-3 at the nuclear envelope and its interaction with plectin. Journal Published:

    PUBLICATION TYPE: Research Support, Non-U.S. Gov

    Journal: Journal of cell science

    VOLUME: 120

    Page Numbers: 3384-94

    Journal Abbreviation: J. Cell. Sci.

    ISSN: 0021-9533

    DAY: 1

    MONTH: Oct

    YEAR: 2007

    Requirements for the localization of nesprin-3 at the nuclear envelope and its interaction with plectin. Information

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    LANGUAGE: eng

    NlmUniqueID: 52457

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    Grant and Affiliation Information for Requirements for the localization of nesprin-3 at the nuclear envelope and its interaction with plectin.

    AFFILIATION: Division of Cell Biology, The Netherlands Cancer Institute, Plesmanlaan 121, 1066 CX Amsterdam, The Netherlands.

    Country: England

    England Research PublicationEngland Research Publication

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    MEDLINETA: J Cell Sci

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