Persistent Link:
http://hdl.handle.net/10150/280545
Title:
Extracellular matrix protein receptors in Drosophila melanogaster
Author:
Futch, Tracy Ann
Issue Date:
2004
Publisher:
The University of Arizona.
Rights:
Copyright © is held by the author. Digital access to this material is made possible by the University Libraries, University of Arizona. Further transmission, reproduction or presentation (such as public display or performance) of protected items is prohibited except with permission of the author.
Abstract:
The extracellular matrix (ECM) is defined as the many different proteins and secreted substances between cells. The ECM plays a major role in the signaling pathways that stimulate cells to perform many varied functions, ranging from control of gene expression at the cellular level to differentiation and development of tissues, organs, and ultimately the entire organism. A portion of this work describes the identification of the division abnormally delayed gene, which encodes a proteoglycan, that is involved in growth factor reception with important developmental consequences in Drosophila melanogaster. The remainder of this work deals with three Drosophila homologs of vertebrate proteins that may interact with integrins, a family of cell surface receptors for extracellular matrix ligands. The three integrin-interacting proteins are referred to by their vertebrate names, and include CD81, a member of the tetraspanin family, ILK, integrin-linked kinase, and CD98hc, a type II transmembrane glycoprotein which is the heavy chain of a multi-protein complex. In this work, the mutant phenotype of CD98hc is larval lethal and not temperature sensitive. Clonal analyses of CD98hc mutants show no phenotype of mutant clones in the eye. Genetic interactions in adult tissues or interactions affecting larval lethality between CD98hc and Drosophila integrin mutants were not observed, and it remains unclear whether CD98hc physically interacts with Drosophila integrins in tissue culture cells. Since no correlation was seen between the interactions of CD98hc and integrins in vertebrate cells and similar putative interactions in flies, this raises the question as to what role, if any, does CD98hc play as an integrin modulator in this organism.
Type:
text; Dissertation-Reproduction (electronic)
Keywords:
Biology, Molecular.
Degree Name:
Ph.D.
Degree Level:
doctoral
Degree Program:
Graduate College; Molecular and Cellular Biology
Degree Grantor:
University of Arizona
Advisor:
Brower, Danny L.

Full metadata record

DC FieldValue Language
dc.language.isoen_USen_US
dc.titleExtracellular matrix protein receptors in Drosophila melanogasteren_US
dc.creatorFutch, Tracy Annen_US
dc.contributor.authorFutch, Tracy Annen_US
dc.date.issued2004en_US
dc.publisherThe University of Arizona.en_US
dc.rightsCopyright © is held by the author. Digital access to this material is made possible by the University Libraries, University of Arizona. Further transmission, reproduction or presentation (such as public display or performance) of protected items is prohibited except with permission of the author.en_US
dc.description.abstractThe extracellular matrix (ECM) is defined as the many different proteins and secreted substances between cells. The ECM plays a major role in the signaling pathways that stimulate cells to perform many varied functions, ranging from control of gene expression at the cellular level to differentiation and development of tissues, organs, and ultimately the entire organism. A portion of this work describes the identification of the division abnormally delayed gene, which encodes a proteoglycan, that is involved in growth factor reception with important developmental consequences in Drosophila melanogaster. The remainder of this work deals with three Drosophila homologs of vertebrate proteins that may interact with integrins, a family of cell surface receptors for extracellular matrix ligands. The three integrin-interacting proteins are referred to by their vertebrate names, and include CD81, a member of the tetraspanin family, ILK, integrin-linked kinase, and CD98hc, a type II transmembrane glycoprotein which is the heavy chain of a multi-protein complex. In this work, the mutant phenotype of CD98hc is larval lethal and not temperature sensitive. Clonal analyses of CD98hc mutants show no phenotype of mutant clones in the eye. Genetic interactions in adult tissues or interactions affecting larval lethality between CD98hc and Drosophila integrin mutants were not observed, and it remains unclear whether CD98hc physically interacts with Drosophila integrins in tissue culture cells. Since no correlation was seen between the interactions of CD98hc and integrins in vertebrate cells and similar putative interactions in flies, this raises the question as to what role, if any, does CD98hc play as an integrin modulator in this organism.en_US
dc.typetexten_US
dc.typeDissertation-Reproduction (electronic)en_US
dc.subjectBiology, Molecular.en_US
thesis.degree.namePh.D.en_US
thesis.degree.leveldoctoralen_US
thesis.degree.disciplineGraduate Collegeen_US
thesis.degree.disciplineMolecular and Cellular Biologyen_US
thesis.degree.grantorUniversity of Arizonaen_US
dc.contributor.advisorBrower, Danny L.en_US
dc.identifier.proquest3132220en_US
dc.identifier.bibrecord.b46711466en_US
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