S. Murty Srinivasula

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Prof. S. Murty Srinivasula
Prof. S. Murty Srinivasula.jpg
Prof. S. Murty Srinivasula
Born1963 (age 59–60)
Nationality Indian
Alma mater
Known forStudies on novel regulators of Apoptosis and Autophagy
Scientific career
Fields Biology, cell biology, apoptosis, autophagy
Institutions

Srinivasa Murty Srinivasula is an Indian cell biologist, a professor at the School of Biology at the Indian Institute of Science Education and Research, Thiruvananthapuram (IISER Thiruvananthapuram) in Kerala, India. His research field is apoptosis, autophagy and oncology. [1] [2]

Contents

Life and career

Professor Murty received his B.Sc and M.Sc degrees from the Andhra University and his PhD from the Banaras Hindu University in Varanasi, India. He later moved to the Thomas Jefferson University as a research associate and became an instructor at the Sidney Kimmel Cancer Center at Thomas Jefferson University in Philadelphia, United States. During 2003–2012, he was the principal investigator at National Cancer Institute, NIH, Bethesda. [3] [4] He was Professor-in-charge (administration) at the IISER Thiruvananthapuram, [5] [6] as well as the member of the IISER TVM Senate. [7] He also served on several institute committees. [8] [9] [10] [11] Currently he is Deputy Director of the institute. [12]

Key awards and distinctions

Professor Murty has received the following awards:

Publications

Professor Murty has published around 100 papers and reviews in international scientific journals. [14]

Key publications

  1. Gan X, Wang J, Wang C, Sommer E, Kozasa T, Srinivasula S, Alessi D, Offermanns S, Simon MI, Wu D. (2012). PRR5L degradation promotes mTORC2-mediated PKC-δ phosphorylation and cell migration downstream of Gα (12). Nat. Cell Biol [15]
  2. Li, P., Nijhawan, D., Budihardjo, I., Srinivasula, S. M., Ahmad, M., Alnemri, E. S., & Wang, X. (1997). Cytochrome c and dATP-Dependent Formation of Apaf-1/Caspase-9 Complex Initiates an Apoptotic Protease Cascade. Cell, 91(4), 479–489. [16]
  3. Fujita K and Srinivasula SM. (2011). TLR4-mediated autophagy in macrophages is a p62-dependent type of selective autophagy of aggresome-like induced structures (ALIS). Autophagy, 7: 29–31. [17]
  4. Fujita K, Xiao Q, Maeda D and Srinivasula SM. (2011). Nrf2-mediated induction of p62 controls TLR4-driven ALIS formation and autophagic degradation, Proc Nat Acad Sci,USA, 108: 1427–32. [18]
  5. Shukla S, Fujita K, Xiao Q, and Srinivasula SM. (2011). A shear stress responsive gene product PP1201 protects against Fas-mediated apoptosis by reducing Fas expression on the cell surface. Apoptosis, 16: 162–173. [19]
  6. Liao, W, Fujita K, Xiao Q, Tchikov V, Yang W, Gunsor, M, Garfield S, Goldsmith, P. El-Deiry WS, Schutze S, and Srinivasula SM. (2009). CARP1 Regulates Induction of NF-κB by TNF-a. Current Biology. 19: R17-R19 [20]
  7. Liao, W, Xiao Q, Tchikov V, Fujita K, Yang W, Wincovitch S, Garfield S, Schutze S, El-Deiry WS, and Srinivasula SM. (2008). CARP-2 is an endosome-associated ubiquitin ligase for RIP and regulates TNF-induced NF-?B activation. Current Biology (article). 18: 641–9. [21]
  8. Srinivasula SM, Jones JM., Datta P., Ji W., Gupta S., Zhang Z., Davies E., Hajnóczky G., Saunders TL., Van Keuren ML., Alnemri T., Meisler ML and Alnemri ES. (2003). Loss of Omi/HtrA2 protease activity causes the neuromuscular disorder of mnd2 mutant mice. Nature. 425: 721–727. [22]
  9. Srinivasula SM, Datta P, Kobayashi M, Wu J-W, Fujioka M, Hegde R, Zhang Z, Mukattash, Fernandes-Alnemri T, Shi Y, Jaynes JB, Alnemri ES. (2002). Sickle, a novel Drosophila death gene in the reaper/hid/grim region encodes an IAP-inhibitory protein. Curr Biol. 12: 125–30. [23]
  10. Srinivasula SM, Hegde R, Saleh A, Datta P, Shiozaki E, Chai J, Lee RA., Robbins PD, Fernandes-Alnemri T, Shi Y., Alnemri ES. (2001). A conserved XIAP-interaction motif in caspase-9 and Smac/Diablo regulates caspase activity and apoptosis. Nature. 410: 112–16. [24]
  11. Srinivasula SM, Saleh A, Balkir L, Robbins PD, and Alnemri ES. (2000). Negative regulation of the Apaf-1 apoptosome by Hsp70. Nature Cell Biol 2: 476–483. [25]

Book chapters

  1. Fujita, K and Srinivasula SM. (2009). Ubiquitination and Death-receptor signaling. Death Receptors and Cognate Ligands in Cancer. Results Probl Cell Differ, SpringerLinks Publisher. 49: 87-114. [26]
  2. Srinivasula SM, Saleh A, Ahmad M, Fernandes-Alnemri T, Alnemri ES. (2001). Isolation and Assay of Caspases. Ch. 1. Methods in Cell Biol. 66:1-27. [27]

Related Research Articles

<span class="mw-page-title-main">Apoptosome</span>

The apoptosome is a large quaternary protein structure formed in the process of apoptosis. Its formation is triggered by the release of cytochrome c from the mitochondria in response to an internal (intrinsic) or external (extrinsic) cell death stimulus. Stimuli can vary from DNA damage and viral infection to developmental cues such as those leading to the degradation of a tadpole's tail.

<span class="mw-page-title-main">BH3 interacting-domain death agonist</span> Protein-coding gene in the species Homo sapiens

The BH3 interacting-domain death agonist, or BID, gene is a pro-apoptotic member of the Bcl-2 protein family. Bcl-2 family members share one or more of the four characteristic domains of homology entitled the Bcl-2 homology (BH) domains, and can form hetero- or homodimers. Bcl-2 proteins act as anti- or pro-apoptotic regulators that are involved in a wide variety of cellular activities.

<span class="mw-page-title-main">Caspase-9</span> Protein-coding gene in the species Homo sapiens

Caspase-9 is an enzyme that in humans is encoded by the CASP9 gene. It is an initiator caspase, critical to the apoptotic pathway found in many tissues. Caspase-9 homologs have been identified in all mammals for which they are known to exist, such as Mus musculus and Pan troglodytes.

<span class="mw-page-title-main">Caspase 8</span> Protein-coding gene in the species Homo sapiens

Caspase-8 is a caspase protein, encoded by the CASP8 gene. It most likely acts upon caspase-3. CASP8 orthologs have been identified in numerous mammals for which complete genome data are available. These unique orthologs are also present in birds.

<span class="mw-page-title-main">Caspase 2</span> Protein-coding gene in the species Homo sapiens

Caspase 2 also known as CASP2 is an enzyme that, in humans, is encoded by the CASP2 gene. CASP2 orthologs have been identified in nearly all mammals for which complete genome data are available. Unique orthologs are also present in birds, lizards, lissamphibians, and teleosts.

<span class="mw-page-title-main">XIAP</span> Protein-coding gene in the species Homo sapiens

X-linked inhibitor of apoptosis protein (XIAP), also known as inhibitor of apoptosis protein 3 (IAP3) and baculoviral IAP repeat-containing protein 4 (BIRC4), is a protein that stops apoptotic cell death. In humans, this protein (XIAP) is produced by a gene named XIAP gene located on the X chromosome.

<span class="mw-page-title-main">Caspase 3</span> Protein-coding gene in the species Homo sapiens

Caspase-3 is a caspase protein that interacts with caspase-8 and caspase-9. It is encoded by the CASP3 gene. CASP3 orthologs have been identified in numerous mammals for which complete genome data are available. Unique orthologs are also present in birds, lizards, lissamphibians, and teleosts.

<span class="mw-page-title-main">Caspase 7</span> Protein-coding gene in the species Homo sapiens

Caspase-7, apoptosis-related cysteine peptidase, also known as CASP7, is a human protein encoded by the CASP7 gene. CASP7 orthologs have been identified in nearly all mammals for which complete genome data are available. Unique orthologs are also present in birds, lizards, lissamphibians, and teleosts.

<span class="mw-page-title-main">Caspase 6</span> Protein-coding gene in the species Homo sapiens

Caspase-6 is an enzyme that in humans is encoded by the CASP6 gene. CASP6 orthologs have been identified in numerous mammals for which complete genome data are available. Unique orthologs are also present in birds, lizards, lissamphibians, and teleosts. Caspase-6 has known functions in apoptosis, early immune response and neurodegeneration in Huntington's and Alzheimer's disease.

<span class="mw-page-title-main">Baculoviral IAP repeat-containing protein 2</span> Protein-coding gene in the species Homo sapiens

Baculoviral IAP repeat-containing protein 2 is a protein that in humans is encoded by the BIRC2 gene.

<span class="mw-page-title-main">Caspase 10</span> Protein-coding gene in the species Homo sapiens

Caspase-10 is an enzyme that, in humans, is encoded by the CASP10 gene.

<span class="mw-page-title-main">Death receptor 5</span> Protein found in humans

Death receptor 5 (DR5), also known as TRAIL receptor 2 (TRAILR2) and tumor necrosis factor receptor superfamily member 10B (TNFRSF10B), is a cell surface receptor of the TNF-receptor superfamily that binds TRAIL and mediates apoptosis.

<span class="mw-page-title-main">Diablo homolog</span> Protein-coding gene in the species Homo sapiens

Diablo homolog (DIABLO) is a mitochondrial protein that in humans is encoded by the DIABLO gene on chromosome 12. DIABLO is also referred to as second mitochondria-derived activator of caspases or SMAC. This protein binds inhibitor of apoptosis proteins (IAPs), thus freeing caspases to activate apoptosis. Due to its proapoptotic function, SMAC is implicated in a broad spectrum of tumors, and small molecule SMAC mimetics have been developed to enhance current cancer treatments.

<span class="mw-page-title-main">APAF1</span> Mammalian protein found in Homo sapiens

Apoptotic protease activating factor 1, also known as APAF1, is a human homolog of C. elegans CED-4 gene.

<span class="mw-page-title-main">BCL10</span> Protein-coding gene in the species Homo sapiens

B-cell lymphoma/leukemia 10 is a protein that in humans is encoded by the BCL10 gene. Like BCL2, BCL3, BCL5, BCL6, BCL7A, and BCL9, it has clinical significance in lymphoma.

<span class="mw-page-title-main">PYCARD</span> Human protein and coding gene

PYCARD, often referred to as ASC, is a protein that in humans is encoded by the PYCARD gene. It is localized mainly in the nucleus of monocytes and macrophages. In case of pathogen infection, however, it relocalizes rapidly to the cytoplasm, perinuclear space, endoplasmic reticulum and mitochondria and it is a key adaptor protein in activation of the inflammasome.

<span class="mw-page-title-main">HtrA serine peptidase 2</span> Enzyme found in humans

Serine protease HTRA2, mitochondrial is an enzyme that in humans is encoded by the HTRA2 gene. This protein is involved in caspase-dependent apoptosis and in Parkinson's disease.

<span class="mw-page-title-main">GSPT1</span> Protein-coding gene in the species Homo sapiens

Eukaryotic peptide chain release factor GTP-binding subunit ERF3A is an enzyme that in humans is encoded by the GSPT1 gene.

<span class="mw-page-title-main">DEDD</span> Protein-coding gene in humans

Death effector domain containing protein is a protein that in humans is encoded by the DEDD gene.

<span class="mw-page-title-main">Early 35 kDa protein</span> Anti-apoptotic viral protein

The Early 35 kDa protein, or P35 in short, is a baculoviral protein that inhibits apoptosis in the cells infected by the virus. Although baculoviruses infect only invertebrates in nature, ectopic expression of P35 in vertebrate animals and cells also results in inhibition of apoptosis, thus indicating a universal mechanism. P35 has been shown to be a caspase inhibitor with a very wide spectrum of activity both in regard to inhibited caspase types and to species in which the mechanism is conserved.

References

  1. ↑ "IRINS Profile page".
  2. ↑ "Google Scholar profile".
  3. ↑ "NIH PI".
  4. ↑ "Linkedin profile".
  5. ↑ "COVID-19: IISER, IIST suspend classes". The Hindu. 14 March 2020. ISSN   0971-751X . Retrieved 26 August 2020.
  6. ↑ "Prof. S. Murty Srinivasula - Personal | IISER Thiruvananthapuram". www.iisertvm.ac.in. Retrieved 26 August 2020.
  7. ↑ "Senate committee".
  8. ↑ "Building and work committee IISER TVM".
  9. ↑ "students_grievance_committee".
  10. ↑ "students_grievance_committee" (PDF).
  11. ↑ "SC/ST cell" (PDF).
  12. ↑ "Deputy Director | IISER Thiruvananthapuram". www.iisertvm.ac.in. Retrieved 17 June 2022.
  13. ↑ "Indian Research Information Network System".
  14. ↑ "INDIAN RESEARCH INFORMATION NETWORK SYSTEM". irins.inflibnet.ac.in. Retrieved 26 August 2020.
  15. ↑ Gan, Xiaoqing; Wang, Jiyong; Wang, Chen; Sommer, Eeva; Kozasa, Tohru; Srinivasula, Srinivasa; Alessi, Dario; Offermanns, Stefan; Simon, Melvin I.; Wu, Dianqing (20 May 2012). "PRR5L degradation promotes mTORC2-mediated PKC-δ phosphorylation and cell migration downstream of Gα12". Nature Cell Biology. 14 (7): 686–696. doi:10.1038/ncb2507. ISSN   1476-4679. PMC   3389271 . PMID   22609986.
  16. ↑ Li, Peng; Nijhawan, Deepak; Budihardjo, Imawati; Srinivasula, Srinivasa M; Ahmad, Manzoor; Alnemri, Emad S; Wang, Xiaodong (November 1997). "Cytochrome c and dATP-Dependent Formation of Apaf-1/Caspase-9 Complex Initiates an Apoptotic Protease Cascade". Cell. 91 (4): 479–489. doi: 10.1016/S0092-8674(00)80434-1 . PMID   9390557.
  17. ↑ Fujita, Ken-Ichi; Srinivasula, Srinivasa M. (May 2011). "TLR4-mediated autophagy in macrophages is a p62-dependent type of selective autophagy of aggresome-like induced structures (ALIS)". Autophagy. 7 (5): 552–554. doi:10.4161/auto.7.5.15101. ISSN   1554-8635. PMC   3127216 . PMID   21412052.
  18. ↑ Fujita, Ken-ichi; Maeda, Daisuke; Xiao, Qi; Srinivasula, Srinivasa M. (25 January 2011). "Nrf2-mediated induction of p62 controls Toll-like receptor-4-driven aggresome-like induced structure formation and autophagic degradation". Proceedings of the National Academy of Sciences of the United States of America. 108 (4): 1427–1432. Bibcode:2011PNAS..108.1427F. doi: 10.1073/pnas.1014156108 . ISSN   1091-6490. PMC   3029726 . PMID   21220332.
  19. ↑ Shukla, Sudhanshu; Fujita, Ken-ichi; Xiao, Qi; Liao, Zhiyong; Garfield, Susan; Srinivasula, Srinivasa M. (25 November 2010). "A shear stress responsive gene product PP1201 protects against Fas-mediated apoptosis by reducing Fas expression on the cell surface". Apoptosis. 16 (2): 162–173. doi:10.1007/s10495-010-0556-y. ISSN   1360-8185. PMC   6993143 . PMID   21107705.
  20. ↑ Liao, Wentao; Fujita, Ken-ichi; Xiao, Qi; Tchikov, Vladimir; Yang, Wensheng; Gunsor, Michele; Garfield, Susan; Goldsmith, Paul; El-Deiry, Wafik S.; Schutze, Stefan; Srinivasula, Srinivasa M. (13 January 2009). "Response: CARP1 regulates induction of NF-κB by TNFα". Current Biology. 19 (1): R17–R19. doi: 10.1016/j.cub.2008.11.041 . ISSN   0960-9822.
  21. ↑ Liao, Wentao; Xiao, Qi; Tchikov, Vladimir; Fujita, Ken-ichi; Yang, Wensheng; Wincovitch, Stephen; Garfield, Susan; Conze, Dietrich; El-Deiry, Wafik S.; Schütze, Stefan; Srinivasula, Srinivasa M. (6 May 2008). "CARP-2 is an endosome-associated ubiquitin ligase for RIP and regulates TNF-induced NF-kappaB activation". Current Biology. 18 (9): 641–649. doi:10.1016/j.cub.2008.04.017. ISSN   0960-9822. PMC   2587165 . PMID   18450452.
  22. ↑ Jones, Julie M.; Datta, Pinaki; Srinivasula, Srinivasa M.; Ji, Weizhen; Gupta, Sanjeev; Zhang, ZhiJia; Davies, Erika; Hajnóczky, György; Saunders, Thomas L.; Van Keuren, Margaret L.; Fernandes-Alnemri, Teresa (16 October 2003). "Loss of Omi mitochondrial protease activity causes the neuromuscular disorder of mnd2 mutant mice". Nature. 425 (6959): 721–727. Bibcode:2003Natur.425..721J. doi:10.1038/nature02052. hdl: 2027.42/62561 . ISSN   1476-4687. PMID   14534547. S2CID   4372496.
  23. ↑ Srinivasula, Srinivasa M.; Datta, Pinaki; Kobayashi, Masatomo; Wu, Jia Wei; Fujioka, Miki; Hegde, Ramesh; Zhang, ZhiJia; Mukattash, Rula; Fernandes-Alnemri, Teresa; Shi, Yigong; Jaynes, James B. (22 January 2002). "sickle, a novel Drosophila death gene in the reaper/hid/grim region, encodes an IAP-inhibitory protein". Current Biology. 12 (2): 125–130. doi:10.1016/s0960-9822(01)00657-1. ISSN   0960-9822. PMC   2743937 . PMID   11818063.
  24. ↑ Srinivasula, S. M.; Hegde, R.; Saleh, A.; Datta, P.; Shiozaki, E.; Chai, J.; Lee, R. A.; Robbins, P. D.; Fernandes-Alnemri, T.; Shi, Y.; Alnemri, E. S. (1 March 2001). "A conserved XIAP-interaction motif in caspase-9 and Smac/DIABLO regulates caspase activity and apoptosis". Nature. 410 (6824): 112–116. Bibcode:2001Natur.410..112S. doi:10.1038/35065125. ISSN   0028-0836. PMID   11242052. S2CID   4380050.
  25. ↑ Saleh, A.; Srinivasula, S. M.; Balkir, L.; Robbins, P. D.; Alnemri, E. S. (August 2000). "Negative regulation of the Apaf-1 apoptosome by Hsp70". Nature Cell Biology. 2 (8): 476–483. doi:10.1038/35019510. ISSN   1465-7392. PMID   10934467. S2CID   20374981.
  26. ↑ Death Receptors and Cognate Ligands in Cancer (PDF). Results and Problems in Cell Differentiation. Vol. 49. 2009. doi:10.1007/978-3-642-03045-1. ISBN   978-3-642-03044-4.
  27. ↑ Srinivasula, Srinivasa M.; Saleh, Ayman; Ahmad, Manzoor; Fernandes-Alnemri, Teresa; Alnemri, Emad S. (1 January 2001). "Chapter 1 Isolation and assay of caspases". Apoptosis. Methods in Cell Biology. Vol. 66. Academic Press. pp. 1–27. doi:10.1016/S0091-679X(01)66002-3. ISBN   9780125441650. PMID   11395999 . Retrieved 19 April 2020.
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