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X-WR-CALDESC:Events for Shi Lab
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BEGIN:VEVENT
DTSTART;TZID=UTC:20230912T080000
DTEND;TZID=UTC:20230912T170000
DTSTAMP:20260504T042807
CREATED:20230913T203718Z
LAST-MODIFIED:20230913T204721Z
UID:1564-1694505600-1694538000@sites.rutgers.edu
SUMMARY:CCB Colloquium – Professor Keith Mickolajczyk\, RWJ Medical School
DESCRIPTION:Single-molecule biophysical approaches to studying the mechanisms of motor proteins\n \nRibosomes are molecular machines made of protein and RNA that translate mRNA into proteins. The biogenesis of new ribosomes is the most energetically costly process in the cell\, accounting for ~60% of all ATP consumed. New ribosomes begin as rRNA\, and are sequentially matured through a complicated multi-step process that involves hundreds of protein factors\, including motor proteins (force-producing enzymes) from the AAA (ATPase associated with diverse cellular activities) and helicase-2 (SF2) superfamilies. Dysregulation of ribosome biogenesis is linked to genetic diseases (ribosomopathies)\, and its upregulation is a hallmark of proliferative cancers. Nonetheless\, the molecular mechanisms underlying ribosome maturation – how motor proteins sequentially convert ribosomal precursors into mature particles – remain poorly understood. Filling this gap in knowledge is essential for understanding ribosomal biology in health and disease\, and for exploring new classes of ribosome biogenesis-targeting chemotherapeutics. \nIn the Mickolajczyk Lab we develop and apply state-of-the-art single-molecule biophysical techniques including optical tweezers\, magnetic tweezers\, FRET\, and label-free imaging to study how AAA and SF2 motor proteins drive ribosome biogenesis. We directly measure how these motors convert the energy from ATP hydrolysis into mechanical work\, and how those forces are then used to change the structure and composition of ribosomal precursors. We further explore how disease-causing mutations in ribosomal proteins alter this fundamental enzymology\, with the ultimate goal of guiding new molecular therapies for ribosomopathies and proliferative cancers.
URL:https://sites.rutgers.edu/shi-lab/event/ccb-colloquium-professor-keith-mickolajczyk-rwj-medical-school/
ATTACH;FMTTYPE=image/jpeg:https://sites.rutgers.edu/shi-lab/wp-content/uploads/sites/378/2023/09/Mickolajczyk_Keith-J-scaled-e1694638036900.jpg
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BEGIN:VEVENT
DTSTART;TZID=UTC:20230914T083000
DTEND;TZID=UTC:20230914T170000
DTSTAMP:20260504T042807
CREATED:20230728T165058Z
LAST-MODIFIED:20230728T165058Z
UID:1549-1694680200-1694710800@sites.rutgers.edu
SUMMARY:Rutgers-Princeton Biomolecular Condensates Day
DESCRIPTION:
URL:https://sites.rutgers.edu/shi-lab/event/rutgers-princeton-biomolecular-condensates-day/
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DTSTART;TZID=UTC:20230919T080000
DTEND;TZID=UTC:20230919T170000
DTSTAMP:20260504T042807
CREATED:20230913T203520Z
LAST-MODIFIED:20230913T204132Z
UID:1562-1695110400-1695142800@sites.rutgers.edu
SUMMARY:CCB Colloquium – Professor Xiaoyang Su\, Rutgers Medical School and Cancer Institute of New Jersey
DESCRIPTION:LC-MS Metabolomics Reveals the Role of SLC45A4 in GABA de novo Synthesis \nAffiliations: 1Departments of Medicine\, Division of Endocrinology\, Robert Wood Johnson Medical School\, Rutgers University; 2Metabolomics Shared Resource\, Rutgers Cancer Institute of New Jersey\, New Brunswick\, NJ 08901\, USA \nSolute carrier (SLC) proteins are membrane transporters that govern the cross-membrane exchanges of glucose\, amino acids\, inorganic ions\, and other small molecule metabolites. Many SLC genes have been shown to be causes of Mendelian diseases in humans\, and a number of SLC transporters are important drug targets. However\, due to myriad technical difficulties\, a large fraction of SLC family members are still orphan transporters without known substrates\, which represents both a significant knowledge gap and a huge opportunity for new drug development.  In order to systematically deorphanize SLC transporters\, we developed a workflow for transcriptomic-metabolomic association analysis. Using this approach\, we identified an uncharacterized gene\, SLC45A4\, that is the single greatest  determinant of  y-aminobutyric acid (GABA) levels in human cancer cells. GABA\, which is mostly known as an inhibitory neurotransmitter in the mammalian central nervous system\, functions in peripheral tissues to regulate cell proliferation\, differentiation\, and migration. Using mass spectrometry and stable isotope tracing\, we found that SLC45A4 increases cellular GABA levels not by promoting GABA uptake but by facilitating GABA de novo synthesis\, suggesting an entirely new regulatory mechanism of GABA synthesis. \nLocation CCB Auditorium (Room 1303)
URL:https://sites.rutgers.edu/shi-lab/event/ccb-colloquium-professor-xiaoyang-su-rutgers-medical-school-and-cancer-institute-of-new-jersey/
ATTACH;FMTTYPE=image/jpeg:https://sites.rutgers.edu/shi-lab/wp-content/uploads/sites/378/2023/09/Photo_Su-scaled-e1694637682660.jpg
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DTSTART;TZID=America/New_York:20230921T110000
DTEND;TZID=America/New_York:20230921T120000
DTSTAMP:20260504T042807
CREATED:20230913T203928Z
LAST-MODIFIED:20230921T165945Z
UID:1569-1695294000-1695297600@sites.rutgers.edu
SUMMARY:Special Seminar – Professor Neha Jain\, Indian Institute of Technology
DESCRIPTION:Modulation of amyloid assembly by chaperone-like proteins \nSoluble proteins have an inherent propensity to undergo altered protein folding\, forming cross-B sheet-rich structures called amyloids. Amyloid fibrils have gained significant attention due to their involvement in neurodegenerative disorders. Parkinson’s disease (PD) is one of the most common movement disorders and the fastest-growing age-related neurological disorder. It is characterized by progressive loss of dopaminergic neurons in substantia nigra due to the accumulation of a-synuclein amyloid fibrils leading to the formation of Lewy bodies. Co-aggregation of a-synuclein with other amyloidogenic proteins such as amyloid-B\, Tau\, and IAPP contributes to the pathophysiology and severity of PD\, suggesting that PD progression is associated with other neurological disorders such as Alzheimer’s and Huntington’s and non-neurological diseases such as Type 2 diabetes and systemic diseases where amyloid deposits can be found in multiple organs including liver\, kidney\, and heart. An intricate machinery of chaperones and chaperone-like proteins keeps a check on protein aggregation and amyloid formation. However\, these guardians lose their properties with age\, and proteins such as a-synuclein accumulate in cells. Understanding the role of chaperone-like proteins as amyloid modulators will help in the early diagnosis of disease and present a novel approach to mitigate amyloid burden in neurodegenerative disease. Using bioinformatics tools\, we have rationally identified human B-sheet rich proteins that have the potential to act as chaperone-like proteins to inhibit amyloid assembly. These proteins possess remarkable structural similarity\, with 50-60% of the structure contributed by B-sheets. We speculated that the B-sheet-rich regions in the proteins may present a scaffold to the growing chain of aggregates\, which is incompetent for maturing into amyloid fibrils. We have taken a multi-disciplinary approach involving microbiology\, biochemistry\, biophysics\, molecular and cellular biology tools to decipher the mechanism of amyloid inhibition by chaperone-like proteins. We demonstrated that sub-stoichiometric ratios of CLP drive a-synuclein into soluble off-pathway aggregates incompetent of making amyloids under in vitro conditions. We believe that unraveling the potential of chaperone-like proteins to alleviate amyloid burden will pave the way for future therapeutics to treat neurodegenerative diseases. \nLocation CCB-3217
URL:https://sites.rutgers.edu/shi-lab/event/special-seminar-professor-neha-jain-indian-institute-of-technology/
LOCATION:CCB 3217
ATTACH;FMTTYPE=image/jpeg:https://sites.rutgers.edu/shi-lab/wp-content/uploads/sites/378/2023/09/Neha-Jain-professional-headshot-scaled-e1694637737488.jpg
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BEGIN:VEVENT
DTSTART;TZID=America/New_York:20230928T110000
DTEND;TZID=America/New_York:20230928T120000
DTSTAMP:20260504T042807
CREATED:20230919T162649Z
LAST-MODIFIED:20230925T141038Z
UID:1577-1695898800-1695902400@sites.rutgers.edu
SUMMARY:Special Seminar – Dr. Charles Cox\, Victor Chang Cardiac Research Institute\, Australia
DESCRIPTION:Discovery and characterization of a novel family of PIEZO channel auxiliary subunits \nPIEZO channels are critical cellular sensors of mechanical forces. Native PIEZO1 channels can display nonuniform subcellular localization and exhibit different gating kinetics—principally\, slower inactivation in many cell types when compared with heterologous expression systems. These observations could be explained by differences in lipid composition\, curvature-dependent sorting or protein-protein interactions. Despite their large size\, ubiquitous expression\, and irreplaceable roles in an ever-growing list of physiological processes\, few PIEZO channel-binding proteins have emerged. Recently using affinity capture mass spectrometry in conjunction with fibroblast cell lines edited using CRISPR/Cas9 we found that MyoD family inhibitor proteins (MDFIC and MDFI)\, interact with both PIEZO1 and PIEZO2 channels. We confirmed using co-immunoprecipitation that these transcriptional regulators\, bind to PIEZO1/2 channels and patch-clamp electrophysiology revealed they regulate channel inactivation. Using single-particle cryo-electron microscopy\, we mapped the interaction site in MDFIC to a lipidated\, C-terminal helix that inserts laterally into the PIEZO1 pore module. These PIEZO interacting proteins fit all the criteria for auxiliary subunits\, contribute to explaining the vastly different gating kinetics of endogenous PIEZO channels observed in many cell types\, shine light on mechanisms potentially involved in human lymphatic vascular disease and pave the way for novel mechano-signaling pathways directly linking PIEZO channels to transcription. \nLocation: CCB-3217 \nZoom Registration
URL:https://sites.rutgers.edu/shi-lab/event/special-seminar-dr-charles-cox-victor-chang-cardiac-research-institute-australia/
LOCATION:CCB 3217
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