Investigating the role of molecular chaperones in neurological diseases

Show simple item record

dc.contributor Caldwell, Guy A.
dc.contributor Churchill, Perry F.
dc.contributor Marcus, Stevan
dc.contributor O'Donnell, Janis M.
dc.contributor Ryals, Phillip E.
dc.contributor.advisor Caldwell, Guy A.
dc.contributor.advisor Churchill, Perry F. Burdette, Alexander Justin 2017-03-01T16:23:48Z 2017-03-01T16:23:48Z 2011
dc.identifier.other u0015_0000001_0000748
dc.identifier.other Burdette_alatus_0004D_10897
dc.description Electronic Thesis or Dissertation
dc.description.abstract Most proteins are elaborate three-dimensional structures comprised of amino acids which form specific interactions with each other to bring about the structure of the protein. Thus, it is no surprise that mutating a single amino acid residue within a protein can completely alter its function or cause it to misfold and prematurely degrade. Given the importance of properly functioning proteins to carry out the daily functions within cells, it is important that these proteins are properly folded and ready to go. Chaperones are proteins that help fold other proteins or play a role in stabilizing them. Absence or mutation of chaperones can lead to devastating diseases or even lethality. TorsinA and NudC are two examples of critical chaperones that are implicated directly, or indirectly, in disease states. TorsinA is a protein that, when mutated, results in early-onset torsion dystonia. NudC on the other hand, plays a role in stabilizing Lis1, which is a causative protein agent of lissencephaly. In this collection of studies, we demonstrate that torsinA is a molecular chaperone capable of binding misfolded proteins directly and maintaining ER homeostasis through ATPase activity and proper ER localization. We also demonstrate that NudC chaperone activity is dependent on dimerization and that this function is conserved between NudC and the closely related NudCL homolog, but not the more distant homolog, NudCL2. Taken together, these studies suggest a possible mechanism for these proteins with respect to their chaperone function and stress the importance of understanding how chaperones function for advancing our understanding of disease.
dc.format.extent 223 p.
dc.format.medium electronic
dc.format.mimetype application/pdf
dc.language English
dc.language.iso en_US
dc.publisher University of Alabama Libraries
dc.relation.ispartof The University of Alabama Electronic Theses and Dissertations
dc.relation.ispartof The University of Alabama Libraries Digital Collections
dc.relation.hasversion born digital
dc.rights All rights reserved by the author unless otherwise indicated.
dc.subject.other Biology
dc.subject.other Biochemistry
dc.subject.other Molecular biology
dc.title Investigating the role of molecular chaperones in neurological diseases
dc.type thesis
dc.type text University of Alabama. Dept. of Biological Sciences Biological Sciences The University of Alabama doctoral Ph.D.

Files in this item

This item appears in the following Collection(s)

Show simple item record

Search DSpace


My Account