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    Light Intermediate Chain 1: a Multifunctional Cargo Binder for Cytoplasmic Dynein 1: a Dissertation

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    Authors
    Wadzinski, Thomas
    Faculty Advisor
    Stephen J. Doxsey, Ph.D.
    Academic Program
    MD/PhD
    UMass Chan Affiliations
    Molecular Medicine
    Document Type
    Doctoral Dissertation
    Publication Date
    2006-09-11
    Keywords
    Dynein ATPase
    Molecular Motors
    Microtubule-Associated Proteins
    Anaphase
    Amino Acids, Peptides, and Proteins
    Cells
    Investigative Techniques
    
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    Abstract
    Cells as dynamic, interactive, and self contained units of life have a need for molecular motors that can create physical forces to move cargoes within the cell. Cytoplasmic dynein 1 is one such molecular motor that has many functions in the cell. The number and variety of functions that involve cytoplasmic dynein 1 suggest that there are a number of different binding sites on dynein for different proteins. Cytoplasmic dynein 1 is a multiprotein complex made up of six different subunit families. The many different combinations of subunits that could be used to make up a cytoplasmic dynein 1 holocomplex provides the variety of different binding sites for cargoes that can be individually regulated. The following chapters flush out how light intermediate chain 1 (LIC1), a subunit of cytoplasmic dynein 1, is involved with multiple dynein functions involving the binding of different cargoes to the cytoplasmic dynein 1 holocomplex, and how the binding of these cargoes can be regulated. First, LIC1 is found to be involved in the spindle assembly checkpoint. LIC1 appears to facilitate the removal of Mad1-Mad2, a complex important in producing a wait anaphase signal, from kinetochores. Second, the involvement of LIC1 in the spindle assembly checkpoint requires the phosphorylation of LIC1 at a putative Cdk1 phosphorylation site. This site is located in a domain of LIC1 that binds various proteins suggesting that this phosphorylation could also regulate these interactions. Third, LIC1 is involved in the centrosomal assembly of pericentrin, an important centrosomal protein. From the data presented herein, LIC1 is shaping up as a multifunctional cargo binder for cytoplasmic dynein 1 that requires regulation of its various cargoes.
    DOI
    10.13028/vnx9-rw27
    Permanent Link to this Item
    http://hdl.handle.net/20.500.14038/31466
    Rights
    Copyright is held by the author, with all rights reserved.
    ae974a485f413a2113503eed53cd6c53
    10.13028/vnx9-rw27
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    Morningside Graduate School of Biomedical Sciences Dissertations and Theses

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