Ramanujan Hegde | |
|---|---|
 Hegde in 2016 | |
| Born | 1 April 1970 |
| Alma mater |
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| Awards | EMBO Member (2013) |
| Scientific career | |
| Fields | Biochemistry |
| Institutions | |
| Thesis | The regulation of protein translocation at the endoplasmic reticulum (1998) |
| Doctoral advisor | Vishwanath R. Lingappa [3] |
| Website | |
Ramanujan Shankar Hegde FRS [4] (born 1 April 1970) [1] is a group leader at the Medical Research Council (MRC) Laboratory of Molecular Biology (LMB). [5] [6]
Hegde was educated at the University of Chicago [2] where he was awarded a Bachelor of Arts degree [1] [ when? ] and the University of California, San Francisco where he was awarded a Doctor of Medicine (MD) degree in 1999 and PhD in 1998 for research on protein targeting and translocation at the endoplasmic reticulum supervised by Vishwanath R. Lingappa. [2] [3]
Hegde's research [7] investigates how proteins are localised correctly inside cells, and how errors during protein maturation are recognised and disposed. These processes are important because the accumulation of abnormal proteins is disruptive to cell function, and underlies numerous diseases. [4]
His laboratory have discovered a widely conserved protein targeting pathway [8] needed by a subset of proteins to reach their correct membrane-embedded destination. Their studies of such protein targeting pathways are revealing how membrane proteins are accurately recognised by the machinery responsible for their proper localisation and insertion. Hegde's work has also shown that even modest failures of individual proteins to reach their correct cellular location can lead to neurodegeneration, and that cells have specialised pathways to identify these wayward proteins and target them for destruction. [4]
As of 2016 [update] , according to Google Scholar [9] his most cited research include papers published in Science , [10] [11] Nature , [12] and Cell . [8] His research has been funded by the Medical Research Council. [13]
Hegde was awarded the R.R. Bensley award in Cell Biology in 2008[ citation needed ] and elected a member of the European Molecular Biology Organisation (EMBO) in 2013. [4] He was also elected a Fellow of the Royal Society (FRS) in 2016. [4]
The endoplasmic reticulum (ER) is, in essence, the transportation system of the eukaryotic cell, and has many other important functions such as protein folding. It is a type of organelle made up of two subunits – rough endoplasmic reticulum (RER), and smooth endoplasmic reticulum (SER). The endoplasmic reticulum is found in most eukaryotic cells and forms an interconnected network of flattened, membrane-enclosed sacs known as cisternae, and tubular structures in the SER. The membranes of the ER are continuous with the outer nuclear membrane. The endoplasmic reticulum is not found in red blood cells, or spermatozoa.
Protein targeting or protein sorting is the biological mechanism by which proteins are transported to their appropriate destinations within or outside the cell. Proteins can be targeted to the inner space of an organelle, different intracellular membranes, the plasma membrane, or to the exterior of the cell via secretion. Information contained in the protein itself directs this delivery process. Correct sorting is crucial for the cell; errors or dysfunction in sorting have been linked to multiple diseases.
A transmembrane domain (TMD) is a membrane-spanning protein domain. TMDs may consist of one or several alpha-helices or a transmembrane beta barrel. Because the interior of the lipid bilayer is hydrophobic, the amino acid residues in TMDs are often hydrophobic, although proteins such as membrane pumps and ion channels can contain polar residues. TMDs vary greatly in size and hydrophobicity; they may adopt organelle-specific properties.
A signal peptide is a short peptide present at the N-terminus of most newly synthesized proteins that are destined toward the secretory pathway. These proteins include those that reside either inside certain organelles, secreted from the cell, or inserted into most cellular membranes. Although most type I membrane-bound proteins have signal peptides, the majority of type II and multi-spanning membrane-bound proteins are targeted to the secretory pathway by their first transmembrane domain, which biochemically resembles a signal sequence except that it is not cleaved. They are a kind of target peptide.
The translocon is a complex of proteins associated with the translocation of polypeptides across membranes. In eukaryotes the term translocon most commonly refers to the complex that transports nascent polypeptides with a targeting signal sequence into the interior space of the endoplasmic reticulum (ER) from the cytosol. This translocation process requires the protein to cross a hydrophobic lipid bilayer. The same complex is also used to integrate nascent proteins into the membrane itself. In prokaryotes, a similar protein complex transports polypeptides across the (inner) plasma membrane or integrates membrane proteins. In either case, the protein complex are formed from Sec proteins, with the heterotrimeric Sec61 being the channel. In prokaryotes, the homologous channel complex is known as SecYEG.
In cell biology, microsomes are heterogeneous vesicle-like artifacts re-formed from pieces of the endoplasmic reticulum (ER) when eukaryotic cells are broken-up in the laboratory; microsomes are not present in healthy, living cells.
A secretory protein is any protein, whether it be endocrine or exocrine, which is secreted by a cell. Secretory proteins include many hormones, enzymes, toxins, and antimicrobial peptides. Secretory proteins are synthesized in the endoplasmic reticulum.
Peter Walter is a German-American molecular biologist and biochemist and is Director of the Bay Area Institute of Science at Altos Labs, Professor at the University of California, San Francisco (UCSF). He was a Howard Hughes Medical Institute (HHMI) Investigator until 2022.
The Medical Research Council (MRC) Laboratory of Molecular Biology (LMB) is a research institute in Cambridge, England, involved in the revolution in molecular biology which occurred in the 1950–60s. Since then it has remained a major medical research laboratory at the forefront of scientific discovery, dedicated to improving the understanding of key biological processes at atomic, molecular and cellular levels using multidisciplinary methods, with a focus on using this knowledge to address key issues in human health.
Endoplasmic-reticulum-associated protein degradation (ERAD) designates a cellular pathway which targets misfolded proteins of the endoplasmic reticulum for ubiquitination and subsequent degradation by a protein-degrading complex, called the proteasome.
The unfolded protein response (UPR) is a cellular stress response related to the endoplasmic reticulum (ER) stress. It has been found to be conserved between mammalian species, as well as yeast and worm organisms.
A target peptide is a short peptide chain that directs the transport of a protein to a specific region in the cell, including the nucleus, mitochondria, endoplasmic reticulum (ER), chloroplast, apoplast, peroxisome and plasma membrane. Some target peptides are cleaved from the protein by signal peptidases after the proteins are transported.
David Ron FRS is a British biochemist.
Sir Hugh Reginald Brentnall Pelham, is a cell biologist who has contributed to our understanding of the body's response to rises in temperature through the synthesis of heat shock proteins. He served as director of the Medical Research Council (MRC) Laboratory of Molecular Biology (LMB) between 2006 and 2018.
Roger Lee Williams is a structural biologist and group leader at the Medical Research Council (MRC) Laboratory of Molecular Biology. His group studies the form and flexibility of protein complexes that associate with and modify lipid cell membranes. His work concerns the biochemistry, structures and dynamics of these key enzyme complexes.
Jan Löwe is a German molecular and structural biologist and the Director of the Medical Research Council (MRC) Laboratory of Molecular Biology (LMB) in Cambridge, UK. He became Director of the MRC-LMB in April 2018, succeeding Sir Hugh Pelham. Löwe is known for his contributions to the current understanding of bacterial cytoskeletons.
Sir Richard Henry Treisman is a British scientist specialising in the molecular biology of cancer. Treisman is a director of research at the Francis Crick Institute in London.
Sean Munro is a Group Leader at the Medical Research Council (MRC) Laboratory of Molecular Biology (LMB). From 2012 until 2023, he served as Head of the Cell Biology Division.
Richard M. Harland is CH Li Distinguished Professor of Genetics, Genomics and Development at the University of California, Berkeley.
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