Material Information

Resolving the functional interaction between IP3R and LRMP
Brennan, Sean
Publication Date:


Subjects / Keywords:
Calcium channels ( jstor )
Cytoskeleton ( jstor )
Eukaryotic cells ( jstor )
Inositols ( jstor )
Membrane proteins ( jstor )
Nuclear interactions ( jstor )
Nuclear lamina ( jstor )
Nuclear membrane ( jstor )
Proteins ( jstor )
Receptors ( jstor )
Membrane proteins
Nuclear membranes
Undergraduate Honors Thesis


Lymphoid-restricted membrane protein (LRMP) is a member of the LINC-complex which connects the nuclear envelope (NE) to the lamina and cytoskeleton in eukaryotic cells. LRMP contains a KASH domain which interacts with SUN-domain proteins and anchors it to the NE. LRMP also contains a coiled-coil domain which binds inositol 1,4,5-triphosphate receptor (IP3R) and recruits it to the outer nuclear membrane (ONM). IP3R forms a tetramer which creates a calcium channel between the endoplasmic reticulum (ER) and the cytoplasm. IP3R was found to interact with LRMP using various regions of its N-terminus and transmembrane domain. When IP3 is present, expression of LRMP leads to a modest increase in calcium release by IP3R; therefore, LRMP positively regulates the activity of IP3R. It was hypothesized that LRMP may recruit phospholipase C beta 2 (PLC-β2), a protein producing IP3, to the NE to bring IP3R and its ligand together and mediate activation of the calcium channel. ( en )
General Note:
Awarded Bachelor of Science; Graduated May 3, 2011 summa cum laude. Major: Microbiology and Cell Science
General Note:
College/School: College of Liberal Arts and Sciences
General Note:
Legacy honors title: Only abstract available from former Honors Program sponsored database.
General Note:
UF Honors Program sponosored database

Record Information

Source Institution:
University of Florida
Rights Management:
Copyright Sean Brennan. Permission granted to the University of Florida to digitize, archive and distribute this item for non-profit research and educational purposes. Any reuse of this item in excess of fair use or other copyright exemptions requires pe