Dr. Veena K Parnaik's research interests are directed towards understanding the functional role of the nuclear lamina, an essential component of nuclear architecture in metazoan cells. She has identified distinctive lamin domains that colocalize with RNA splicing factor compartments and are involved in the spatial organization of transcription and pre-mRNA splicing. She has shown that the internal lamina is reorganized specifically during muscle differentiation in a process mediated by cyclin D3 and pRb. Interestingly, cyclin D3 can bind directly to lamin A; this supports the emerging concept that lamins influence specific signalling pathways by sequestration of key regulatory factors. Her studies demonstrate that lamin A mutations impair muscle differentiation and DNA repair pathways and current work is aimed at addressing how this occurs. Dr. Parnaik`s findings have given important mechanistic insights into the role of lamin mutations in debilitating inherited diseases that affect muscle tissues and cause progerias.
RI Kumaran, Bh Muralikrishna and VK Parnaik, Lamin A/C speckles mediate spatial organization of splicing factor compartments and RNA polymerase II transcription J. Cell Biol. 159, 783-793 (2002).
I Mariappan and VK Parnaik, Sequestration of pRb by cyclin D3 causes intranuclear reorganization of lamin A/C during muscle cell differentiation Mol. Biol. Cell 16, 1948-1960 (2005).
K Manju, Bh Muralikrishna, VK Parnaik, Expression of disease-causing lamin A mutants impairs the formation of DNA repair foci J. Cell Sci. 119, 2704-2714 (2006).
VK Parnaik, Role of nuclear lamins in nuclear organization, cellular signaling and inherited diseases Int. Rev. Cell Mol. Biol. 266, 157-206 (2008).
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|Lamin C and chromatin organization in Drosophila||J. Genetics, 89:37-49||2010|
|Lamin A rod mutants target heterochromatin protein 1a and b for proteasomal degradation by activation of F-box protein, FBXW10||PLoS ONE, 5:e10620||2010|
|Differential dynamics and stability of lamin A rod domain mutants||Int. J. Integrative Biol., 5:1-8||2009|
|Role of nuclear lamins in nuclear organization, cellular signaling and inherited diseases||Int. Rev. Cell Mol. Biol., 266:157-206||2008|
|Differential dynamics of splicing factor SC35 during the cell cycle||J. Biosci., 33:345-354||2008|
|Delay-induced transient increase and heterogeneity in gene expression in negatively auto-regulated gene circuits||PloS ONE, 3:e2972||2008|
|Lamin A Ser404 Is a Nuclear Target of Akt Phosphorylation in C2C12 Cells||J. Proteome Res., 7:4727-4735||2008|
|Identification of cyclin D3 as a new interaction partner of lamin A/C||Biochem. Biophys. Res. Comm., 355:981-985||2007|
|A pathogenic mechanism leading to partial lipodystrophy and prospects for pharmacological treatment of insulin resistance syndrome||Acta Biomed.., 78:207-215||2007|
|Expression of disease-causing lamin A mutants impairs the formation of DNA repair foci||J. Cell Sci., 119:2704-2714||2006|
|An essential GT motif in the lamin A promoter mediates activation by CREB-binding protein||Biochem. Biophys. Res. Comm., 348:1132-1137||2006|
|Laminopathies: multiple disorders arising from defects in nuclear architecture||J. Biosci., 31:405-421||2006|
|Sequestration of pRb by cyclin D3 causes intranuclear reorganization of lamin A/C during muscle cell differentiation||Mol. Biol. Cell., 16:1948-1960||2005|
|Altered pre-lamin A processing is a common mechanism leading to lipodystrophy||Hum. Mol. Genet., 14:1489-1502||2005|
|Rescue of heterochromatin organization in Hutchinson-Gilford progeria by drug treatment||Cell. Mol. Life Sci., 62:2669-2678||2005|
|Immunolocalization of detergent-susceptible nucleoplasmic lamin A/C foci by a novel monoclonal antibody||J. Cell. Biochem., 91: 730-739||2004|
|Cell-type specific interactions at regulatory motifs in the first intron of the lamin A gene||FEBS Lett., 568:122-128||2004|
|Heat-stress induced alterations in localization of small heat shock proteins in mouse myoblasts: intranuclear lamin A/C speckles as target for ?B-crystallin and hsp 25||Exp. Cell Res., 299:393-403||2004|
|Failure of lamin A/C to functionally assemble in R482L mutated familial partial lipodystrophy fibroblasts: Altered intermolecular interaction with emerin and implications for gene transcription||Exp. Cell Res.., 291:122-134||2003|
|Lamin A/C speckles mediate spatial organization of splicing factor compartments and RNA polymerase II transcription||J. Cell Biol., 159:783-793||2002|
|Early localization of NPA58, a rat nuclear pore-associated protein, to the reforming nuclear envelope during mitosis||J Biosci., 26:47-55||2001|
|Novel Sp family-like transcription factors are present in adult insect cells and are involved in transcription from the polyhedrin gene initiator promoter||J Biol. Chem., 276:23440-23449||2001|
|Sp3 and AP-1 mediate transcriptional activation of the lamin A proximal promoter||Eur. J. Biochem., 268:3736-3743||2001|
|Distinct changes in intranuclear lamin A organization during myoblast differentiation||J. Cell Sci., 114:4001-4011||2001|
|Phosphorylation of NPA58, a rat nuclear pore-associated protein, correlates with its mitotic distribution||Exp. Cell. Res., 261:199-208||2000|