About CCMB



Scientist Details


Contact Details


Name : Veena K Parnaik

Room : E205

Telephone :
040-27192614,27160222

Fax :
040-27160311, 27160591

E-mail :
veenap@ccmb.res.in


Research Interests

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.



Selected Publications

  • G Jagatheesan, S Thanumalayan, Bh Muralikrishna, N Rangaraj, A A Karande and V K Parnaik, “Colocalization of intranuclear lamin foci with RNA splicing factors” J. Cell Sci. 112, 4651-4661 (1999).

  • 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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