Show simple item record

dc.contributor.advisorFrank B. Gertler.en_US
dc.contributor.authorKuhlmann, Georgiana L. (Georgiana Louise)en_US
dc.contributor.otherMassachusetts Institute of Technology. Dept. of Biology.en_US
dc.date.accessioned2010-09-02T17:25:30Z
dc.date.available2010-09-02T17:25:30Z
dc.date.copyright2010en_US
dc.date.issued2010en_US
dc.identifier.urihttp://hdl.handle.net/1721.1/58294
dc.descriptionThesis (S.M.)--Massachusetts Institute of Technology, Dept. of Biology, 2010.en_US
dc.descriptionCataloged from PDF version of thesis.en_US
dc.descriptionIncludes bibliographical references (p. 47-57).en_US
dc.description.abstractIn metastatic cancer, cells must be able to migrate from their original environment, move through the blood or lymphatic system, and colonize a distant organ. Mena, a member of the Ena/VASP family of proteins, is upregulated in invasive populations of breast cancer cells. The Ena/VASP (enabled/vasodilator-stimulated phosphoprotein) family of proteins regulate both the geometry and dynamics of actin filament networks. Mena specifically is alternatively spliced with an invasive isoform, MenaINV, upregulated in metastastic cells, while an epithelial isoform, Menalla, is downregulated. SH2- domain containing 5-inositol phosphatase (SHIP2) interacts with Mena and is thought to play a role in breast cancer. SHIP2 is a 5-phosphatase that catalyzes the dephosphorylation of phosphatidylinositol 3,4,5-trisphosphate (PI(3,4,5)P 3) to phosphatidylinositol 3,4-bisphosphate (PI(3,4)P2) as well as the dephosphorylation of phosphatidylinositol 4,5- bisphosphate (PI(4,5)P 2). PI(3,4,5)P 3 and P][(4,5)P 2 are two major phosphoinositides at the plasma membrane and regulate a variety of cellular functions, including receptor signaling, membrane-cytoskeleton interactions and clathrin-mediated endocytosis. Here I have looked at the effects of knocking down SHIP2 in the MTLn3 cell line, a metastatic rat breast carcinoma line. I found that when SHIP2 is knocked down in cells, there is an increase in membrane protrusion upon stimulation with EGF, and that recruitment of Mena to the leading edge is enhanced, implying that this increase in protrusion may be due to a change in Mena localization.en_US
dc.description.statementofresponsibilityby Georgiana L. Kuhlmann.en_US
dc.format.extent57 p.en_US
dc.language.isoengen_US
dc.publisherMassachusetts Institute of Technologyen_US
dc.rightsM.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.en_US
dc.rights.urihttp://dspace.mit.edu/handle/1721.1/7582en_US
dc.subjectBiology.en_US
dc.titleThe 5' inositol phosphatase SHIP2 regulates EGF-elicited protrusion in MTLn3 cellsen_US
dc.title.alternativeEffects of SHIP2 knockdown in MTLn3 cellsen_US
dc.typeThesisen_US
dc.description.degreeS.M.en_US
dc.contributor.departmentMassachusetts Institute of Technology. Dept. of Biology.en_US
dc.contributor.departmentMassachusetts Institute of Technology. Department of Biology
dc.identifier.oclc654432791en_US


Files in this item

Thumbnail

This item appears in the following Collection(s)

Show simple item record