Seetharaman Parashuraman

ORCID: 0000-0001-5113-4592
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About
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Research Areas
  • Cellular transport and secretion
  • Lipid Membrane Structure and Behavior
  • Endoplasmic Reticulum Stress and Disease
  • Glycosylation and Glycoproteins Research
  • Lysosomal Storage Disorders Research
  • Cystic Fibrosis Research Advances
  • Sphingolipid Metabolism and Signaling
  • Photoreceptor and optogenetics research
  • Asthma and respiratory diseases
  • Trace Elements in Health
  • Allergic Rhinitis and Sensitization
  • Bioinformatics and Genomic Networks
  • Erythrocyte Function and Pathophysiology
  • Autophagy in Disease and Therapy
  • Pancreatic function and diabetes
  • Biomedical Research and Pathophysiology
  • Photosynthetic Processes and Mechanisms
  • Gene Regulatory Network Analysis
  • Dermatology and Skin Diseases
  • Amino Acid Enzymes and Metabolism
  • Advanced Electron Microscopy Techniques and Applications
  • Galectins and Cancer Biology
  • Mast cells and histamine
  • Cancer, Stress, Anesthesia, and Immune Response
  • IL-33, ST2, and ILC Pathways

National Research Council
2013-2024

Institute for Experimental Endocrinology and Oncology
2021-2024

National Research Council
2023

Institute of Cell Biology and Neurobiology
2019-2021

Institute of Protein Biochemistry
2013-2020

Center for Excellence in Molecular Cell Science
2019

National Academies of Sciences, Engineering, and Medicine
2019

Telethon Institute Of Genetics And Medicine
2013-2015

Mario Negri Sud Foundation
2014

National Institute of Immunology
2001-2011

TANGO1 (transport and Golgi organization 1) interacts with CTAGE5 COPII components Sec23/Sec24 recruits ERGIC-53 (endoplasmic reticulum [ER]–Golgi intermediate compartment 53)–containing membranes to generate a mega-transport carrier for export of collagens apolipoproteins from the ER. We now show that TANGO1, at ER, assembles in ring encircles components. The C-terminal, proline-rich domains molecules are initially tilted onto coats but appear be pushed apart as grows. These findings lend...

10.1083/jcb.201608080 article EN cc-by-nc-sa The Journal of Cell Biology 2017-03-09

The mechanism of transport through the Golgi complex is not completely understood, insofar as no single appears to account for all observations. Here, we compare soluble secretory proteins (albumin and α1-antitrypsin) with that supramolecular cargoes (e.g., procollagen) are proposed traverse by compartment progression–maturation. We show these much faster than procollagen while moving same stack. Moreover, present kinetic morphological observations indicate albumin occurs diffusion via...

10.7554/elife.02009 article EN cc-by eLife 2014-05-27

The unconventional secretory pathway exports proteins that bypass the endoplasmic reticulum. In Saccharomyces cerevisiae, conditions trigger Acb1 secretion via this generate a Grh1 containing compartment composed of vesicles and tubules surrounded by cup-shaped membrane collectively called CUPS. Here we report quantitative assay for reveals requirements ESCRT-I, -II, -III but, surprisingly, without involvement Vps4 AAA-ATPase. major ESCRT-III subunit Snf7 localizes transiently to CUPS was...

10.7554/elife.16299 article EN cc-by eLife 2016-04-26

After leaving the endoplasmic reticulum, secretory proteins traverse several membranous transport compartments before reaching their destinations. How they move through Golgi complex, a major station composed of stacks cisternae, is central yet unsettled issue in membrane biology. Two classes mechanisms have been proposed. One based on cargo-laden carriers hopping across stable cisternae and other "maturing" that carry cargo forward while progressing stack. A key difference between two...

10.1083/jcb.201211147 article EN cc-by-nc-sa The Journal of Cell Biology 2013-06-17

Article13 September 2021Open Access Source DataTransparent process GRASP55 regulates intra-Golgi localization of glycosylation enzymes to control glycosphingolipid biosynthesis Prathyush Pothukuchi orcid.org/0000-0002-6242-2319 Institute Biochemistry and Cell Biology, National Research Council Italy, Rome, Italy Search for more papers by this author Ilenia Agliarulo These authors contributed equally work Marinella Pirozzi Riccardo Rizzo Domenico Russo Gabriele Turacchio Julian Nüchel...

10.15252/embj.2021107766 article EN cc-by-nc-nd The EMBO Journal 2021-09-13

Wilson disease (WD) is an autosomal recessive disorder that caused by the toxic accumulation of copper (Cu) in liver. The ATP7B gene, which mutated WD, encodes a multitransmembrane domain adenosine triphosphatase traffics from trans‐Golgi network to canalicular area hepatocytes, where it facilitates excretion excess Cu into bile. Several mutations, including H1069Q and R778L are two most frequent variants, result protein products, which, although still functional, remain endoplasmic...

10.1002/hep.28398 article EN cc-by-nc Hepatology 2015-12-14

The flat Golgi cisterna is a highly conserved feature of eukaryotic cells, but how this morphology achieved and it related to its function in cargo sorting export? A physical model led us propose that sphingomyelin (SM) metabolism at the trans-Golgi membranes mammalian cells essentially controls structural features by regulating association curvature-generating proteins. An experimental test hypothesis revealed affecting SM homeostasis converted cisternae into curled with concomitant...

10.7554/elife.24603 article EN cc-by eLife 2017-05-13

Rab-GTPase regulates the fusion between two specific vesicles. It is well documented that, for their biological function, Rab proteins need to be prenylated attachment vesicle membrane. In contrast, we showed in present investigation that SopE, a type III secretory protein of Salmonella, translocates onto Salmonella-containing phagosomes (LSP) and mediates recruitment non-prenylated Rab5 (Rab5:DeltaC4) on LSP GTP form. Simultaneously, SopE infected cell cytosol acts as an Rab5-specific...

10.1074/jbc.m101034200 article EN cc-by Journal of Biological Chemistry 2001-06-01

Significance Proteins are modified by many posttranslational modifications (PTMs) with crucial regulatory functions. A PTM attracting increasing interest is ADP-ribosylation, capable of altering cellular targets. We show that mono-ADP-ribosylation PARP12 the protein Golgin-97 regulates transport to plasma membrane a specific group functionally cargo proteins. shown be part cascade initiated PKD and involving direct phosphorylation activation PARP12. These events define, through...

10.1073/pnas.2026494119 article EN cc-by-nc-nd Proceedings of the National Academy of Sciences 2021-12-30

Cystic fibrosis (CF) is caused by mutations in CF transmembrane conductance regulator (CFTR). The most frequent mutation (F508del-CFTR) results altered proteostasis, that is, the misfolding and intracellular degradation of protein. F508del-CFTR proteostasis machinery its homeostatic regulation are well studied, while question whether ‘classical’ signalling pathways phosphorylation cascades might control remains barely explored. Here, we have unravelled acting selectively on...

10.7554/elife.10365 article EN cc-by eLife 2015-12-22

Thymic stromal lymphopoietin (TSLP), mainly expressed by epithelial cells, plays a central role in asthma. In humans, TSLP exists two variants: the long form (lfTSLP) and shorter isoform (sfTSLP). Macrophages (HLMs) mast cells (HLMCs) are close proximity human lung play key roles We evaluated early proteolytic effects of tryptase chymase released HLMCs on mass spectrometry. also investigated whether its fragments generated these enzymes induce angiogenic factor release from HLMs. Mass...

10.3390/ijms25074049 article EN International Journal of Molecular Sciences 2024-04-05

Previously, we showed that live Salmonella-containing phagosomes(LSP) recruit early acting Rab5 and promote fusion with endosomes, thus avoiding transport to the lysosomes. Therefore, Salmonellasurvive in a specialized compartment. Here show scavenger-receptor-mediated intracellular delivery of muramyl dipeptide (MDP)to macrophages leads efficient killing Salmonella both vitro vivo. To understand trafficking modulation by MDP, investigated levels endocytic Rab proteins, which are major...

10.1242/jcs.00034 article EN Journal of Cell Science 2002-09-15
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