2026-09-19T03:29:15Zhttps://dspace.mit.edu/server/oai/request

oai:dspace.mit.edu:1721.1/986302026-06-16T18:15:07Zcom_1721.1_7582com_1721.1_7581col_1721.1_131022

Frank B. Gertler. Riquelme, Daisy N. (Daisy Noelia) Massachusetts Institute of Technology. Department of Biology. Massachusetts Institute of Technology. Department of Biology 2015-09-17T19:00:52Z 2015-09-17T19:00:52Z 2015 2015 http://hdl.handle.net/1721.1/98630 920672950 Thesis: Ph. D., Massachusetts Institute of Technology, Department of Biology, 2015. Cataloged from PDF version of thesis. Includes bibliographical references. EnaNASP proteins have an established role in regulating actin dynamics in diverse cell types. The mammalian EnaNASP family members, Mena, VASP, and EVL have many overlapping activities. However, the three family members are not equivalent and each possess a number of features that are absent in the others. Unique modes of regulation and paralog-specific interacting partners point to potential differences in the activity and function of EnaNASP proteins. The function of this family of proteins relies on their ability to form tetramers via a highly conserved tetramerization domain located at the Cterminus of all EnaNASP proteins. The potential formation of mixed tetramers may combine the unique aspects of each paralog into one molecule. Here, I describe a series of immunoprecipitation experiments to evaluate hetero-oligomerization of EnaNASP proteins in a controlled setting. My data demonstrate that VASP can form hetero-oligomers with itself, Mena, and EVL without bias. However, the assembly of Mena and EVL hetero-tetramers is disfavored. In addition, I find that the tetramerization domain mediates the observed selectivity in complex formation. My findings suggest that hetero-tetramerization serve as an additional method to regulate the activity of EnaNASP proteins. by Daisy N. Riquelme. Ph.D. 157 pages eng Massachusetts Institute of Technology M.I.T. 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. See provided URL for inquiries about permission. http://dspace.mit.edu/handle/1721.1/7582 Biology. Selectivity in subunit composition of EnaNASP tetramers Selective formation of mixed Ena/VASP tetramers Thesis application/pdf false Publication unknown unknown <Publication xmlns="https://www.openaire.eu/cerif-profile/1.1/" id="fe089a30-3dba-4c2e-a409-a7200b2baae1"> <Type xmlns="https://www.openaire.eu/cerif-profile/vocab/COAR_Publication_Types">http://purl.org/coar/resource_type/c_1843</Type> <Language>eng</Language> <Title>Selectivity in subunit composition of EnaNASP tetramers</Title> <Subtitle>Selective formation of mixed Ena/VASP tetramers</Subtitle> <PublishedIn> <Publication> </Publication> </PublishedIn> <PublicationDate>2015</PublicationDate> <Authors> <Author> <DisplayName>Riquelme, Daisy N. (Daisy Noelia)</DisplayName> <Affiliation> <OrgUnit> </OrgUnit> </Affiliation> </Author> </Authors> <Editors> </Editors> <Publishers> <Publisher> <DisplayName>Massachusetts Institute of Technology</DisplayName> <OrgUnit /> </Publisher> </Publishers> <License>http://dspace.mit.edu/handle/1721.1/7582</License> <Keyword>Biology.</Keyword> <Abstract>EnaNASP proteins have an established role in regulating actin dynamics in diverse cell types. The mammalian EnaNASP family members, Mena, VASP, and EVL have many overlapping activities. However, the three family members are not equivalent and each possess a number of features that are absent in the others. Unique modes of regulation and paralog-specific interacting partners point to potential differences in the activity and function of EnaNASP proteins. The function of this family of proteins relies on their ability to form tetramers via a highly conserved tetramerization domain located at the Cterminus of all EnaNASP proteins. The potential formation of mixed tetramers may combine the unique aspects of each paralog into one molecule. Here, I describe a series of immunoprecipitation experiments to evaluate hetero-oligomerization of EnaNASP proteins in a controlled setting. My data demonstrate that VASP can form hetero-oligomers with itself, Mena, and EVL without bias. However, the assembly of Mena and EVL hetero-tetramers is disfavored. In addition, I find that the tetramerization domain mediates the observed selectivity in complex formation. My findings suggest that hetero-tetramerization serve as an additional method to regulate the activity of EnaNASP proteins.</Abstract> <Access xmlns="http://purl.org/coar/access_right" > </Access> </Publication>