Atin K. Mandal, Ph.D

Asstt. Professor
Division of Molecular Medicine
Ph.D: Bose Institute, Jadavpur University (2000)

 Tel: 91-33-2569-3237
Fax:  91-33-2355-3886

E-mail: mandalak@bic.boseinst.ernet.in
            atink99@yahoo.com



Research interest

 

Protein quality control is an essential cellular process that maintains protein homeostasis or proteostasis. Maintaining proper balance between folding and degradation of misfolded proteins is critical for cell survival. Molecular chaperones facilitate polypeptide folding by protecting newly synthesized or misfolded proteins against aggregation. They also promote degradation of unfolded or misfolded proteins by the ubiquitin-proteasome pathway. This quality control process plays a vital role in several pathophysiological conditions including cancer, diabetes and late-onset neurological diseases. My focus of research is to understand the mechanism of cellular protein quality control.

 

Objectives:

 ·          Molecular mechanism of cytosolic protein quality control

·          Crosstalk between molecular chaperones and ubiquitin ligases in quality control of misfolded proteins

·          Develop inhibitors of molecular chaperones

Publications (in last 10 years):

 

1.      Nillegoda, N.B., Theodoraki M.A, Mandal, A.K., Mayo, K.J., Ren, H.Y., Sultana, R., Wu, K., Johnson, J., Cyr, D.M., Caplan, A.J.  Ubr1 and Ubr2 function in a quality control pathway for degradation of unfolded cytosolic proteins.  Molecular Biology of Cell 2010 May 12. [Epub ahead of print]

 

2.      Mandal, A.K.*, Gibney PA*, Nillegoda, N.B., Theodoraki M.A, Morano KA. and Caplan A.J. Hsp110 chaperones control client fate determination in the Hsp70-Hsp90 chaperone system. Molecular Biology of Cell 21, 1439-1448, 2010 (*joint first authors)

 

3.      Mandal, A.K., Nillegoda, N., Chen, J., and Caplan, A. J. Ydj1 protects nascent protein kinases from degradation and controls the rate of their maturation. Molecular and Cellular Biology 28(13), 4434-4444, 2008

 

4.      Mandal, A.K., Lee, P., Chen, J., Nillegoda, N., Heller, H., DiStasio, S., Oen, H., Victor, J., Nair, N.M., Brodsky, J.L and Caplan, A. J. Cdc37 has distinct roles in protein kinase quality control that protects nascent chains from degradation and promotes post-translational maturation. Journal of Cell Biology. 176, 319-328, 2007

 

5.      Caplan, A J., Mandal, A K., Theodoraki, M A.  Molecular chaperones and protein kinase quality control. Trends in Cell Biology.17(2), 87-92, 2007

 

6.      Robzyk, K., Oen, H., Buchanan, G., Butler L.M., Tilley, W., Mandal, A. K., Rosen, N., and Caplan, A.J. Uncoupling of Hormone-dependence from chaperone-dependence in the L701H mutation of the androgen receptor. Mol. Cell. Endocrinol.  268 (1-2):67-74, 2007

7.      Ying, Y., Mandal, A.K., Bredeston, L.M, Gonzalez-Flecha, F.L. and Argüello, J.M. Activation of Archaeoglobus fulgidus Cu+-ATPase CopA by cysteine. Biochim. Biophys. Acta. 1768, 495-501, 2007

8.      Sazinsky, M.H., Mandal, A.K., Argüello, J.M., and Rosenzweig A.C. Structure of the ATP binding domain from the Archaeoglobus fulgidus Cu+-ATPase. J. Biol. Chem. 281, 11161-11166, 2006

9.      Mandal, A.K., Yang, Y., Kertesz, T.M., and Argüello, J.M. Identification of the transmembrane metal binding site in Cu+ transporting P1B-type ATPases. J. Biol. Chem. 279, 54802-54807, 2004

 10.  Mana-Capelli, S., Mandal, A.K., and Argüello, J.M. Archaeoglobus fulgidus CopB is a thermophilic Cu2+-ATPase. Functional role of its His-rich N-terminal metal binding domain. J. Biol. Chem. 278, 40534-40541, 2003

11.  Mandal, A.K., and Argüello, J.M. Functional roles of metal binding domains of the Archaeoglobus fulgidus Cu+-ATPase CopA. Biochemistry 42, 11040-11047, 2003

12.  Mandal, A.K., Cheung W., and Argüello, J.M. Characterization of a thermophilic P-type Ag+/Cu+ -ATPase from the extremophile Archaeoglobus fulgidus. J. Biol. Chem. 277, 7201-7208, 2002

13.  Mikhaylova, L., Mandal, A.K., and Argüello, J.M. The catalytic phosphorylation of the Na,K-ATPase drives the outward movement of the cation-binding H5-H6 hairpin. Biochemistry 41(25) 8195-8202, 2002

14.  Mandal, A.K., Roy, K., Sil, P.C., Yadav, S.P. and Sen, P.C. Purification, characterization and partial amino acid sequencing of a 70 kD inhibitor protein of Na+, K+-ATPase from goat testis cytosol. Mol. Cell. Biochem. 223, 7-14, 2001

 

Book Chapters

 

1.      Mandal, A.K., Nair, D.M., and Caplan, A.J. Role of Cdc37 in protein kinase folding.   In:“Protein Reviews” Vol 7: Cell Stress Proteins (Edited by Stuart K. Calderwood) Springer. 326-337, 2007

2.      Mandal, A.K., Mikhaylova, L., and Argüello, J.M.  S5-H5 helix in the Na,K-ATPase: A structural link between phosphorylation and cation-binding sites. In: "The Na,K-ATPase and Related Cation Pumps" (Jorgensen, P.L., Maunsbach, A.B., and S.J.D., Karlish, Eds.) Annals. New York Acad. Sc. 224-225, 2003

 

3.      Argüello, J.M., Mandal, A.K., and Mana-Capelli, S. Heavy metal transport CPx-ATPases from the thermophile Archaeoglobus fulgidus. In: "The Na,K-ATPase and Related Cation Pumps" (Jorgensen, P.L., Maunsbach, A.B., and S.J.D., Karlish, Eds.) Annals. New York Acad. Sc. 212-218, 2003

 

Professional Societies

 

        New York Academy of Sciences 

        American Society of Cell Biology