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Coauthors
Rituraj Marwaha Department of Biological Sciences, Indian Institute of Science Education and Research Mohali (IISERM), India, India,
1 protocol

Mahak Sharma
  • Department of Biological Sciences, Indian Institute of Science Education and Research Mohali (IISERM), India, India,
  • 1 Author merit

Education

Ph.D. in Biochemistry and Molecular Biology, Department of Biochemistry and Molecular Biology, University of Nebraska Medical Center, USA, 2009

Current position

Assistant Professor and Wellcome/DBT India Alliance Intermediate Fellow, Department of Biological Sciences, Indian Institute of Science Education and Research (IISER) Mohali, India

Publications

  1. https://scholar.google.co.in/citations?user=Mjc8UUUAAAAJ&hl=en
  2. Marwaha, R., Arya, S., Jagga, D., Kaur, H., Tuli, A. and Sharma, M. (2017). The Rab7 effector PLEKHM1 binds Arl8b to promote cargo traffic to lysosomes. J Cell Biol.
  3. Sharma, M. and Caplan, S. (2016). BAR domains and BAR domain superfamily proteins. In: Bradshaw, R. A. and Stahl, P. D. (Eds). Encyclopedia of cell biology, Elsevier 2: 491-502.
  4. Khatter, D., Raina, V. B., Dwivedi, D., Sindhwani, A., Bahl, S. and Sharma, M. (2015). The small GTPase Arl8b regulates assembly of the mammalian HOPS complex on lysosomes. J Cell Sci 128(9): 1746-1761.
  5. Khatter, D., Sindhwani, A. and Sharma, M. (2015). Arf-like GTPase Arl8: Moving from the periphery to the center of lysosomal biology. Cell Logist 5(3): e1086501.
  6. Tuli, A., Thiery, J., James, A. M., Michelet, X., Sharma, M., Garg, S., Sanborn, K. B., Orange, J. S., Lieberman, J. and Brenner, M. B. (2013). Arf-like GTPase Arl8b regulates lytic granule polarization and natural killer cell-mediated cytotoxicity. Mol Biol Cell 24(23): 3721-3735.
  7. Garg, S., Sharma, M., Ung, C., Tuli, A., Barral, D. C., Hava, D. L., Veerapen, N., Besra, G. S., Hacohen, N. and Brenner, M. B. (2011). Lysosomal trafficking, antigen presentation, and microbial killing are controlled by the Arf-like GTPase Arl8b. Immunity 35(2): 182-193.
  8. Peters, H. L., Tuli, A., Sharma, M., Naslavsky, N., Caplan, S., MacDonald, R. G. and Solheim, J. C. (2011). Regulation of major histocompatibility complex class I molecule expression on cancer cells by amyloid precursor-like protein 2. Immunol Res 51(1): 39-44.
  9. Kieken, F., Sharma, M., Jovic, M., Giridharan, S. S., Naslavsky, N., Caplan, S. and Sorgen, P. L. (2010). Mechanism for the selective interaction of C-terminal Eps15 homology domain proteins with specific Asn-Pro-Phe-containing partners. J Biol Chem 285(12): 8687-8694.
  10. Sharma, M., Giridharan, S. S., Rahajeng, J., Caplan, S. and Naslavsky, N. (2010). MICAL-L1: An unusual Rab effector that links EHD1 to tubular recycling endosomes. Commun Integr Biol 3(2): 181-183.
  11. Jovic, M., Sharma, M., Rahajeng, J. and Caplan, S. (2010). The early endosome: a busy sorting station for proteins at the crossroads. Histol Histopathol 25(1): 99-112.
  12. Pant, S., Sharma, M., Patel, K., Caplan, S., Carr, C. M. and Grant, B. D. (2009). AMPH-1/Amphiphysin/Bin1 functions with RME-1/Ehd1 in endocytic recycling. Nat Cell Biol 11(12): 1399-1410.
  13. Sharma, M., Giridharan, S. S., Rahajeng, J., Naslavsky, N. and Caplan, S. (2009). MICAL-L1 links EHD1 to tubular recycling endosomes and regulates receptor recycling. Mol Biol Cell 20(24): 5181-5194.
  14. Tuli, A., Sharma, M., Capek, H. L., Naslavsky, N., Caplan, S. and Solheim, J. C. (2009). Mechanism for amyloid precursor-like protein 2 enhancement of major histocompatibility complex class I molecule degradation. J Biol Chem 284(49): 34296-34307.
  15. Tuli, A., Sharma, M., Wang, X., Simone, L. C., Capek, H. L., Cate, S., Hildebrand, W. H., Naslavsky, N., Caplan, S. and Solheim, J. C. (2009). Amyloid precursor-like protein 2 association with HLA class I molecules. Cancer Immunol Immunother 58(9): 1419-1431.
  16. Sharma, M., Jovic, M., Kieken, F., Naslavsky, N., Sorgen, P. and Caplan, S. (2009). A model for the role of EHD1-containing membrane tubules in endocytic recycling. Commun Integr Biol 2(5): 431-433.
  17. Tuli, A., Sharma, M., McIlhaney, M. M., Talmadge, J. E., Naslavsky, N., Caplan, S. and Solheim, J. C. (2008). Amyloid precursor-like protein 2 increases the endocytosis, instability, and turnover of the H2-K(d) MHC class I molecule. J Immunol 181(3): 1978-1987.
  18. Tuli, A., Sharma, M., Naslavsky, N., Caplan, S. and Solheim, J. C. (2008). Specificity of amyloid precursor-like protein 2 interactions with MHC class I molecules. Immunogenetics 60(6): 303-313.
  19. Sharma, M., Naslavsky, N. and Caplan, S. (2008). A role for EHD4 in the regulation of early endosomal transport. Traffic 9(6): 995-1018.
  20. Sharma, M., Jovic, M. and Caplan, S. (2007). Epidermal growth factor receptor protein tyrosine kinase substrate (Eps15). Targeted Proteins Database (TPdb).
  21. Naslavsky, N., Rahajeng, J., Sharma, M., Jovic, M. and Caplan, S. (2006). Interactions between EHD proteins and Rab11-FIP2: a role for EHD3 in early endosomal transport. Mol Biol Cell 17(1): 163-177.
1 Protocol published
DQ-Red BSA Trafficking Assay in Cultured Cells to Assess Cargo Delivery to Lysosomes
Authors:  Rituraj Marwaha and Mahak Sharma, date: 10/05/2017, view: 1347, Q&A: 0
Lysosomes are the terminal end of the endocytic pathway having acidic environment required for active hydrolases that degrade the cargo delivered to these compartments. This process of cargo delivery and degradation by endo-lysosomes is a tightly ...