Regulation of HnRNP LL by the depolarization/CaMKIV pathway

dc.contributor.authorMahmood, Niaz
dc.contributor.examiningcommitteeLeygue, Etienne (Biochemistry and Medical Genetics) Soussi Gounni, Abdel (Immunology)en_US
dc.contributor.supervisorXie, Jiuyong (Biochemistry and Medical Genetics)en_US
dc.date.accessioned2015-09-28T19:36:17Z
dc.date.available2015-09-28T19:36:17Z
dc.date.issued2015
dc.degree.disciplineBiochemistry and Medical Geneticsen_US
dc.degree.levelMaster of Science (M.Sc.)en_US
dc.description.abstractThe RNA binding protein heterogeneous nuclear ribonucleoprotein L-Like (hnRNP LL) is known to regulate the alternative splicing of various physiologically important precursor messenger RNAs (pre-mRNAs). It undergoes a wide range of post-translational modifications (PTMs), including phosphorylation, ubiquitination and acetylation. However, the target amino acids and effects of these PTMs on the functions of hnRNP LL have not been characterized so far. In this study, we show for the first time that the endogenous hnRNP LL is phosphorylated upon depolarization. Using phosphopeptide mapping followed by the generation of a custom-made phospho-site specific antibody, we further show that phosphorylation at Ser308 of hnRNP LL is induced by depolarization though it is probably not the major phospho-amino acid target of depolarization/CaMKIV. The residue is critical for the nuclear localization and its phosphorylation essential for the CaMKIV-caused perinucleolar localization of the hnRNP LL protein in HEK293T cells. The residue is likely also critical in the regulation of nuclear functions like pre-mRNA splicing.en_US
dc.description.noteFebruary 2016en_US
dc.identifier.urihttp://hdl.handle.net/1993/30847
dc.language.isoengen_US
dc.rightsopen accessen_US
dc.subjectHnRNP LLen_US
dc.titleRegulation of HnRNP LL by the depolarization/CaMKIV pathwayen_US
dc.typemaster thesisen_US
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