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Please use this identifier to cite or link to this item: http://hdl.handle.net/1807/18858

Title: Identification of Novel Interacting Proteins of Four and a Half LIM Domains Protein 1 from Human Embryonic Kidney 293 Cells
Authors: Shathasivam, Thiruchelvi
Advisor: Gramolini, Anthony
Department: Physiology
Keywords: protein interactions
protein purification
Issue Date: 15-Feb-2010
Abstract: Four and a half LIM domains protein 1 (FHL1), consisting of 4.5 protein interaction mediating LIM domains, is a predominantly skeletal muscle protein that has consistently been upregulated in a variety of cardiovascular diseases. Since proteins mediate their functions in conjunction with other proteins, it was considered that delineation of interactions would provide insight into FHL1’s regulation and regulatory functions. We performed tandem affinity purification (TAP) from human embryonic kidney 293 (HEK-293) cells to purify tagged FHL1 and interacting proteins. Samples were analyzed using gel-free liquid chromatography mass spectrometry (LC-MS). 61 high confidence potential interactors were identified from multiple experiments. Validation of interactions was then performed by co-immunoprecipitation (co-IP) or streptavidin bead pull down, and supported by immunofluorescent colocalization studies. FHL1 interactions could thus be supported for four novel candidates: non-muscle α-actinin 1 (ACTN1), PDZ and LIM domain protein 1 (PDLIM1), cytoplasmic gelsolin (GSN), and ryanodine receptor 1 (RYR1).
URI: http://hdl.handle.net/1807/18858
Appears in Collections:Master
Department of Physiology - Master theses

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