Ofer Moldavski
University of California, Berkeley
18 Papers
1 Citations
Ofer Moldavski is an academic researcher from University of California, Berkeley. The author has contributed to research in topics: Lipogenesis & Liver X receptor. The author has an hindex of 7, co-authored 9 publications. Previous affiliations of Ofer Moldavski include Hebrew University of Jerusalem & Massachusetts Institute of Technology.
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Papers
Lysosomal cholesterol activates mTORC1 via an SLC38A9-Niemann-Pick C1 signaling complex
Brian M. Castellano,Ashley M. Thelen,Ofer Moldavski,McKenna Feltes,Reini E. N. van der Welle,Laurel Mydock-McGrane,Xuntian Jiang,Robert J. van Eijkeren,Oliver B. Davis,Sharon M. Louie,Rushika M. Perera,Douglas F. Covey,Daniel K. Nomura,Daniel S. Ory,Roberto Zoncu +14 more
TL;DR: Cholesterol is identified, an essential building block for cellular growth, as a nutrient input that drives mTORC1 recruitment and activation at the lysosomal surface and the SLC38A9-NPC1 complex, which is key to the ability of m TORC1 to respond to variations in dietary lipid supply.
Confinement to Organelle-Associated Inclusion Structures Mediates Asymmetric Inheritance of Aggregated Protein in Budding Yeast
Rachel Spokoini,Ofer Moldavski,Yaakov Nahmias,Jeremy L. England,Maya Schuldiner,Daniel Kaganovich +5 more
TL;DR: It is shown that misfolded proteins are retained in the mother cell by being sequestered in juxtanuclear quality control compartment (JUNQ) and insoluble protein deposit (IPOD) inclusions, which are attached to organelles.
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Lipid Droplets Are Essential for Efficient Clearance of Cytosolic Inclusion Bodies
Ofer Moldavski,Triana Amen,Smadar Levin-Zaidman,Miriam Eisenstein,Ilana Rogachev,Alexander Brandis,Daniel Kaganovich,Maya Schuldiner +7 more
TL;DR: It is shown that IBs and LDs are spatially and functionally linked, and a mechanism for IB clearance via a sterol-based metabolite emanating from LDs is demonstrated, uncovering a function for Iml2 andLDs in regulating a critical stage of cellular proteostasis.
119
A nutrient-induced affinity switch controls mTORC1 activation by its Rag GTPase-Ragulator lysosomal scaffold.
Rosalie E. Lawrence,Kelvin F. Cho,Ronja Rappold,Anna Thrun,Marie Tofaute,Do Jin Kim,Ofer Moldavski,James H. Hurley,Roberto Zoncu +8 more
TL;DR: It is shown that mTORC1 capture and activation at the lysosome are regulated by nutrients that destabilize Rag GTPase–Ragulator binding, and delineate how cancer-specific Rag mutants increase m TORC1 signalling.
The Hetero-Hexameric Nature of a Chloroplast AAA+ FtsH Protease Contributes to Its Thermodynamic Stability
TL;DR: In silico study with mixed models of FtsH2/5 suggests that heteromeric hexamer structure with ratio of 4∶2 is more likely to exists, and biochemical data corroborate the in silico model and suggest that the thylakoid Ftsh hexamer is composed of two ‘type A’ and four ‘ type B’ subunits.