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dc.contributor.advisorLee, Myeongwoo.
dc.contributor.authorAhn, Jeong H.
dc.contributor.otherBaylor University. Dept. of Biology.en
dc.date.accessioned2009-03-31T15:39:15Z
dc.date.available2009-03-31T15:39:15Z
dc.date.copyright2008-12
dc.date.issued2009-03-31T15:39:15Z
dc.identifier.urihttp://hdl.handle.net/2104/5275
dc.descriptionIncludes bibliographical references (p. 43-48).en
dc.description.abstractNPXY (Asn-Pro-X-Tyr) is a conserved tyrosine phosphorylation motif that binds to PTB (phospho-tyrosine binding) domain of other protein. Integrins, a heterodimeric cell surface receptor for extracellular matrix (ECM), include two NPXY motifs in tandem on the cytoplasmic tails of β subunits. I generated a tyrosine to glutamate mutation mimicking constitutive phosphorylation of NPXY in βpat-3 integrin of Caenorhabditis elegans. The transgenic animals displayed disorganized muscle actin and abnormal gonad migration and tail morphology, suggesting that the phosphorylation of tyrosine causes defective phenotypes. In addition, the transgenic animals produced the high number of males, implying that the transgenic animals are similar to him-4/hemicentin alleles and that the lack of him-4 may cause the phosphorylation of NPXY. Genetic analyses revealed that tyrosine to phenylalanine mutations in both positions, βpat-3(YYFF), was able to suppress high incidence in male, mating ability, and egg-laying phenotypes of him-4 mutant, suggesting that a function of him-4 is to prevent the phosphorylation of βpat-3 NPXY. Taken together, our data suggest that changes in the ECM regulate the phosphorylation of the integrin NPXY.en
dc.description.statementofresponsibilityby Jeong H. Ahn.en
dc.format.extentvi, 48 p. : ill.en
dc.format.extent281443 bytes
dc.format.extent762475 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypeapplication/pdf
dc.language.isoen_USen
dc.rightsBaylor University theses are protected by copyright. They may be viewed from this source for any purpose, but reproduction or distribution in any format is prohibited without written permission. Contact librarywebmaster@baylor.edu for inquiries about permission.en
dc.subjectTyrosine.en
dc.subjectIntegrins.en
dc.subjectExtracellular matrix.en
dc.subjectCellular signal transduction.en
dc.subjectGenetic regulation.en
dc.subjectCaenorhabditis elegans -- Physiology.en
dc.subjectPhosphorylation.en
dc.titleThe functional analysis of NPXY motif in β integrin in vivo.en
dc.typeThesisen
dc.description.degreeM.S.en
dc.rights.accessrightsWorldwide accessen
dc.contributor.departmentBiology.en


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