Jeffrey E. Gerst

ORCID: 0000-0002-8411-6881
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About
Contact & Profiles
Research Areas
  • RNA Research and Splicing
  • Fungal and yeast genetics research
  • Cellular transport and secretion
  • RNA and protein synthesis mechanisms
  • Endoplasmic Reticulum Stress and Disease
  • RNA modifications and cancer
  • Plant Reproductive Biology
  • RNA Interference and Gene Delivery
  • melanin and skin pigmentation
  • Neurobiology and Insect Physiology Research
  • Lipid Membrane Structure and Behavior
  • Lysosomal Storage Disorders Research
  • Protein Kinase Regulation and GTPase Signaling
  • Extracellular vesicles in disease
  • Ubiquitin and proteasome pathways
  • Peroxisome Proliferator-Activated Receptors
  • Bacterial Genetics and Biotechnology
  • RNA regulation and disease
  • Molecular Biology Techniques and Applications
  • Mitochondrial Function and Pathology
  • Phytochemicals and Antioxidant Activities
  • Biofuel production and bioconversion
  • Parkinson's Disease Mechanisms and Treatments
  • Microbial Metabolic Engineering and Bioproduction
  • Genomics and Chromatin Dynamics

Weizmann Institute of Science
2016-2025

Child Trends
2010-2022

MRC Cancer Unit
2010

Cold Spring Harbor Laboratory
1990-2010

Stanford University
2010

Brandeis University
2010

European Molecular Biology Organization
2010

Ludwig Cancer Research
2010

Yale University
2010

University of Oregon
2010

Targeted mRNA localization is a likely determinant of localized protein synthesis. To investigate whether mRNAs encoding mitochondrial proteins (mMPs) localize to mitochondria and, thus, might confer synthesis and import, we visualized endogenously expressed mMPs in vivo for the first time. We determined 24 yeast matrix, outer inner membrane, intermembrane space found that many colocalize with vivo. This supports earlier cell fractionation microarray-based studies proposed mMP association...

10.1261/rna.2621111 article EN RNA 2011-06-24

Significance mRNA molecules convey genetic information within cells, beginning from genes in the nucleus to ribosomes cell body, where they are translated into proteins. Here we show a mode of transferring one another. Contrary previous publications suggesting that mRNAs transfer via extracellular vesicles, provide visual and quantitative data showing membrane nanotubes direct cell-to-cell contact. We predict this process has major role regulating local cellular environments with respect...

10.1073/pnas.1706365114 article EN cc-by-nc-nd Proceedings of the National Academy of Sciences 2017-10-24

Genome duplication in eukaryotes created paralog pairs of ribosomal proteins (RPs) that show high sequence similarity/identity. However, individual paralogs can confer vastly different effects upon cellular processes, e.g., specific yeast regulate actin organization, bud site selection, and mRNA localization, although how specificity is conferred unknown. Changes the RP composition ribosomes might allow for specialized translation subsets mRNAs, yet it unclear whether exist if controls...

10.1083/jcb.201706059 article EN cc-by-nc-sa The Journal of Cell Biology 2017-11-08

CAP, a protein from Saccharomyces cerevisiae that copurifies with adenylyl cyclase, appears to be required for yeast cells fully responsive RAS proteins. CAP also normal cell morphology and responsiveness nutrient deprivation excess. We describe here molecular phenotypic analysis of the protein. The N-terminal domain is necessary sufficient cellular response activated protein, while C-terminal responses extremes. Thus, novel example bifunctional component involved in regulation diverse...

10.1128/mcb.11.3.1248 article EN Molecular and Cellular Biology 1991-03-01

We have identified an open reading frame on chromosome XI of the yeast, Saccharomyces cerevisiae, as encoding a protein with phospholipase D (PLD) activity. named this frame, PLD1, and show that yeast bearing disruption in gene are unable to catalyze hydrolysis phosphatidylcholine. PLD1 encodes hypothetical 1683 amino acids has predicted molecular mass 195 kDa. Yeast disruptions at locus morphologically normal grow vegetatively like wild-type cells. In contrast, homozygous Δpld1 diploid...

10.1074/jbc.271.5.2361 article EN cc-by Journal of Biological Chemistry 1996-02-01

Members of the synaptobrevin/VAMP family v-SNAREs are thought to be essential for vesicle docking and exocytosis in both lower higher eukaryotes. Here, we describe yeast mutants that appear bypass known v-SNARE requirement secretion. Recessive mutations either VBM1 or VBM2, which encode related ER-localized membrane proteins, allow grow normally secrete absence Snc v-SNAREs. These show selective alterations protein transport, resulting differential trafficking secretion certain cargo. Yet,...

10.1083/jcb.143.5.1167 article EN The Journal of Cell Biology 1998-11-30

SNC1, a gene from the yeast Saccharomyces cerevisiae, encodes homolog of vertebrate synaptic vesicle-associated membrane proteins (VAMPs) or synaptobrevins. SNC1 was isolated by its ability to suppress loss CAP function in S. cerevisiae strains possessing an activated allele RAS2. is component RAS-responsive adenylyl cyclase complex. The N-terminal domain required for full cellular responsiveness RAS proteins. C-terminal normal morphology and nutrient extremes. Multicopy plasmids expressing...

10.1073/pnas.89.10.4338 article EN Proceedings of the National Academy of Sciences 1992-05-15

Polarized growth in the budding yeast Saccharomyces cerevisiae depends upon asymmetric localization and enrichment of polarity secretion factors at membrane prior to budding. We examined how these (i.e., Cdc42, Sec4, Sro7) reach bud site found that their respective mRNAs localize tip incipient nuclear division. Asymmetric mRNA facilitate ASH1 (e.g., 3′ untranslated region, She proteins 1 5, Puf6, actin cytoskeleton, a physical association with She2). placement precedes protein subsequent...

10.1128/mcb.01643-06 article EN Molecular and Cellular Biology 2007-03-06

We have identified, cloned, and studied a gene, cap, encoding protein that is associated with adenylyl cyclase in the fission yeast Schizosaccharomyces pombe. This shares significant sequence homology cyclase-associated CAP Saccharomyces cerevisiae. bifunctional protein; N-terminal domain appears to be involved cellular responsiveness RAS, whereas loss of C-terminal portion morphological nutritional defects. S. pombe cap can suppress phenotypes deletion cerevisiae but does not domain....

10.1091/mbc.3.2.167 article EN Molecular Biology of the Cell 1992-02-01

Intracellular mRNA targeting and localized translation are potential determinants for protein localization. To facilitate targeting, mRNAs possess specific cis -acting sequence motifs that recognized by trans RNA-binding proteins (RBPs). While many trafficked, our knowledge of the RBPs involved presence additional transcripts within these ribonucleoprotein (RNP) complexes is limited. identification bind to mRNAs, we developed R N A -binding p rotein purification id entification (RaPID), a...

10.1261/rna.2091710 article EN RNA 2010-09-28

mRNAs encoding secreted/membrane proteins (mSMPs) are believed to reach the endoplasmic reticulum (ER) in a translation-dependent manner confer protein translocation. Evidence exists, however, for translation- and signal recognition particle (SRP)-independent mRNA localization ER, suggesting that there alternate paths RNA delivery. We localized endogenously expressed mSMPs yeast using an aptamer-based RNA-tagging procedure fluorescence microscopy. Unlike polarity secretion factors colocalize...

10.1091/mbc.e13-01-0038 article EN cc-by-nc-sa Molecular Biology of the Cell 2013-08-01

Targeted mRNA trafficking and local translation may play a significant role in controlling protein localization. Here we examined for the first time localization of all ( approximately 50) mRNAs encoding peroxisomal proteins (mPPs) involved peroxisome biogenesis function. By using bacteriophage MS2-CP RNA-binding (RBP) fused to multiple copies GFP, demonstrated that >40 endogenously expressed mPPs tagged with MS2 aptamer form fluorescent RNA granules vivo. The use different RFP-tagged...

10.1073/pnas.0910754106 article EN Proceedings of the National Academy of Sciences 2009-11-11

Upon amino acid (AA) starvation and TOR inactivation, plasma-membrane-localized permeases rapidly undergo ubiquitination internalization via the vacuolar protein sorting/multivesicular body (VPS-MVB) pathway are degraded in yeast vacuole. We now show that specific Golgi proteins also directed to vacuole under these conditions as part of a quality-control (GQC) process. The degradation GQC substrates is dependent upon by defective-for-SREBP-cleavage (DSC) complex, which was identified genetic...

10.1016/j.celrep.2015.08.026 article EN cc-by-nc-nd Cell Reports 2015-09-01

Full-length mRNAs transfer between adjacent mammalian cells via direct cell-to-cell connections called tunneling nanotubes (TNTs). However, the extent of mRNA at transcriptome-wide level (the 'transferome') is unknown. Here, we analyzed transferome in an vitro human-mouse cell co-culture model using RNA-sequencing. We found that non-selective, prevalent across human transcriptome, and amount to mouse embryonic fibroblasts (MEFs) strongly correlates with endogenous gene expression donor...

10.7554/elife.83584 article EN cc-by eLife 2023-05-30

Analysis of single-molecule fluorescent in situ hybridization (smFISH) images is important to translate cellular image data into a quantifiable format. Although smFISH the gold standard for RNA localization measurements, there are no freely available, user-friendly applications assaying messenger (mRNA) organelles. EASI-ORC (Efficient and Segmentation Images Organelle-RNA Colocalization) novel pipeline automated analysis multiple yeast cells. automates segmentation cells organelles,...

10.1038/s42003-025-07682-z article EN cc-by-nc-nd Communications Biology 2025-02-15
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