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Functional analysis of RAB-10 and its interacting partner EHBP-1 during endocytosis in the Caenorhabditis elegans intestine
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Chen, Chih-Hsiung. Functional analysis of RAB-10 and its interacting partner EHBP-1 during endocytosis in the Caenorhabditis elegans intestine. Retrieved from https://doi.org/doi:10.7282/T3V40VN3

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Uniform TitleFunctional analysis of RAB-10 and its interacting partner EHBP-1 during endocytosis in the Caenorhabditis elegans intestine
NameChen, Chih-Hsiung (author); Driscoll, Monica (chair); Grant, Barth (internal member); Rongo, Christopher (internal member); Kramer, Sunita (outside member); ; Rutgers University; Graduate School - New Brunswick
Date Created2007
Other Date2007 (degree)
SubjectCell and Developmental Biology, Caenorhabditis elegans, Endocytosis
Extentxxii, 288 pages
DescriptionThe endocytic pathway of eukaryotes is essential for the internalization and trafficking of macromolecules, fluid, membranes, and membrane proteins. One of the most enigmatic aspects of this process is endocytic recycling, the return of macromolecules (often receptors) and fluid from endosomes to the plasma membrane. It has been previously shown that the EH-domain protein RME-1 is a critical regulator of endocytic recycling in worms and mammals. In my studies, the RAB-10 protein was identified as a key regulator of endocytic recycling upstream of RME-1 in polarized epithelial cells of the Caenorhabditis elegans intestine. rab-10 null mutant intestinal cells accumulate abnormally abundant RAB-5-positive early endosomes, some of which are enlarged by more than 10-fold. Conversely most RME-1-positive recycling endosomes are lost in rab-10 mutants. The abnormal early endosomes in rab-10 mutants accumulate basolaterally recycling transmembrane cargo molecules and basolaterally recycling fluid, consistent with a block in basolateral transport. These results indicate a role for RAB-10 in basolateral recycling upstream of RME-1.
In a yeast two-hybrid screen for RAB-10-interacting proteins, eight candidates with RAB-10-interacting ability were identified. They are EHBP-1, HUM-2, GCK-2, CNT-1, F52E1.13, Y82E9BR.21, ZK1248.10, and F20D1.2. In addition, 5/8 candidates identified interacted with RAB-8 and RAB-10 but not with RAB-5, -7, -11, or -35 in the two-hybrid assay. One of the RAB-10-interacting candidates, EHBP-1, an actin-cyskeleton bundling protein, was revealed to function together with RAB-10 in vivo. Knockdown of EHBP-1 function by RNAi produced a rab-10-like phenotype in the intestine. In addition, EHBP-1 was found to be required for endosomal membrane association of RAB-10 and actin association with the enlarged endosomes of rab-10 mutants. I conclude that RAB-10 and EHBP-1 likely function together in basolateral endocytic recycling pathway of the C. elegans intestine.
NotePh.D.
NoteIncludes bibliographical references (p. 272-286).
Genretheses, ETD doctoral
Persistent URLhttps://doi.org/doi:10.7282/T3V40VN3
LanguageEnglish
CollectionGraduate School - New Brunswick Electronic Theses and Dissertations
Organization NameRutgers, The State University of New Jersey
RightsThe author owns the copyright to this work.
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