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Membrane remodeling by novel regulators of the recycling endosome

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TypeOfResource
Text
TitleInfo (ID = T-1)
Title
Membrane remodeling by novel regulators of the recycling endosome
SubTitle
the RME-1 and AMPH-1 partnership
PartName
PartNumber
NonSort
Identifier (displayLabel = ); (invalid = )
ETD_2398
Identifier (type = hdl)
http://hdl.rutgers.edu/1782.2/rucore10001600001.ETD.000052268
Language (objectPart = )
LanguageTerm (authority = ISO639-2); (type = code)
eng
Genre (authority = marcgt)
theses
Subject (ID = SBJ-1); (authority = RUETD)
Topic
Cell and Developmental Biology
Subject (ID = SBJ-2); (authority = ETD-LCSH)
Topic
Cell membranes
Subject (ID = SBJ-3); (authority = ETD-LCSH)
Topic
Endosomes
Abstract
Endocytic recycling is the process where by molecules traffic from endosomes back to the plasma membrane. This process is crucial for the maintenance of cellular homeostasis and cell polarity. C. elegans RME-1 and its mammalian homolog mRme-1/EHD1 are required for exit of cargo from the recycling endosome. The mechanism by which they control cargo exit has led to a proposal that they may function in formation of carrier tubules that break off from the recycling endosome. Recent studies suggested parallels of EHD family to the Dynamin GTPase superfamily of mechanoenzymes which function in membrane fission at the clathrin coated pit. Through a bioinformatics based screen we identified an interaction between RME-1 and AMPH-1, the only C. elegans member of Amphiphysin/BIN1 family of BAR-domain proteins. In mammalian neuronal synapses, Amphiphysin family proteins regulate the recruitment and activity of Dynamin for formation of vesicles. We established that AMPH-1 co localizes with RME-1 on recycling endosomes in vivo, amph-1 deletion mutants are defective in recycling endosome morphology and function and that AMPH-1 and RME-1 cooperatively promote the recycling of transmembrane cargo. in vitro we found that purified recombinant AMPH-1/RME-1 co-assemble on membranes to produce short, coated tubules which are qualitatively distinct from those produced by either protein alone. We have established that AMPH-1 and RME-1 serve as a novel membrane tubulation and possibly fission machinery at the recycling endosome, an interaction that is conserved in mammals.
We also investigated the function of a serine/threonine kinase of the germinal center kinase family (GCK-2) which is known to bind two Rabs, RAB-10 and RAB-8, which function in endocytic recycling. We established that GCK-2 is a novel effector of RAB-8 in regulating RME-1 labeled recycling endosomes. In select functions, it may serve as a RAB-10 effector. This may be an example of RABs being sequentially activated by binding the same effector. This study identifies a novel function for a germinal center kinase proteins whose only known function relates to the MAPK signaling cascade.
We recently established an interaction between GCK-2 and AMPH-1. We hypothesize that this interaction could serve as a hub which ties together the major recycling endosome interactions mapped for RME-1/AMPH-1 as well as with RAB-8/RAB-10.
PhysicalDescription
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electronic resource
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xiii, 305 p. : ill.
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Note (type = degree)
Ph.D.
Note (type = bibliography)
Includes bibliographical references (p. 292-304)
Note (type = statement of responsibility)
by Saumya Pant
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Pant
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Saumya
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1979-
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Saumya Pant
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Rongo
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Christopher
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chair
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Advisory Committee
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Christopher Rongo
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Grant
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Barth
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internal member
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Advisory Committee
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Barth D Grant
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Driscoll
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Monica
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Monica Driscoll
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Matsumura
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Fumio
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Fumio Matsumura
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Carr
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Chavela
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Advisory Committee
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Chavela M Carr
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Rutgers University
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degree grantor
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Graduate School - New Brunswick
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school
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2010
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2010-01
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xx
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Title
Rutgers University Electronic Theses and Dissertations
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ETD
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Graduate School - New Brunswick Electronic Theses and Dissertations
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rucore19991600001
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NjNbRU
Identifier (type = doi)
doi:10.7282/T3SN093V
Genre (authority = ExL-Esploro)
ETD doctoral
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Rights

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The author owns the copyright to this work.
Copyright
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Copyright protected
Notice
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Availability
Status
Open
Reason
Permission or license
Note
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Pant
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Saumya
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2010-01-05 15:45:01
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Saumya Pant
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Rutgers University. Graduate School - New Brunswick
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I hereby grant to the Rutgers University Libraries and to my school the non-exclusive right to archive, reproduce and distribute my thesis or dissertation, in whole or in part, and/or my abstract, in whole or in part, in and from an electronic format, subject to the release date subsequently stipulated in this submittal form and approved by my school. I represent and stipulate that the thesis or dissertation and its abstract are my original work, that they do not infringe or violate any rights of others, and that I make these grants as the sole owner of the rights to my thesis or dissertation and its abstract. I represent that I have obtained written permissions, when necessary, from the owner(s) of each third party copyrighted matter to be included in my thesis or dissertation and will supply copies of such upon request by my school. I acknowledge that RU ETD and my school will not distribute my thesis or dissertation or its abstract if, in their reasonable judgment, they believe all such rights have not been secured. I acknowledge that I retain ownership rights to the copyright of my work. I also retain the right to use all or part of this thesis or dissertation in future works, such as articles or books.
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730 days
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