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David D. Sabatini

Researcher at New York University

Publications -  122
Citations -  18170

David D. Sabatini is an academic researcher from New York University. The author has contributed to research in topics: Endoplasmic reticulum & Golgi apparatus. The author has an hindex of 59, co-authored 119 publications receiving 17814 citations. Previous affiliations of David D. Sabatini include Rockefeller University & Yale University.

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Hydrolysis of GTP on rab11 is required for the direct delivery of transferrin from the pericentriolar recycling compartment to the cell surface but not from sorting endosomes.

TL;DR: The incapacity of the constitutively active form of rab11 (Q70L) to inhibit recycling of molecules interiorized at 16 degreesC is consistent with their recycling taking place directly from sorting endosomes, in a process that does not require hydrolysis of GTP on rab11.
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Asymmetric budding of viruses in epithelial monlayers: a model system for study of epithelial polarity.

TL;DR: Because different viruses select specific domains of plasma membrane in the same cell type, virus-infected epithelial monolayers can provide an excellent model system for studies of the mechanisms that generate regional differences in the distribution of plasma membranes components of epithelial cells.
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Actin microfilaments play a critical role in endocytosis at the apical but not the basolateral surface of polarized epithelial cells.

TL;DR: There is a fundamental difference in the process by which endocytic vesicles are formed at the two surfaces of polarized epithelial cells and that the integrity and/or the polymerization of actin filaments are required at the apical surface.
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Synthesis and incorporation of myelin polypeptides into CNS myelin.

TL;DR: It was found that crude myelin fractions are highly enriched in mRNAs coding for the MBPs but not in mRNA coding for PLP, which suggests that whereas the bound polysomes synthesizing PLP are largely confined to the cell body, free polysome synthesizing MBPs are concentrated in oligodendrocyte processes involved in myelination, which explains the immediate incorporation of MBPs into the developing myelin sheath.
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Regulation of mTORC1 by the Rag GTPases is necessary for neonatal autophagy and survival

TL;DR: The Rag GTPases signal glucose and amino-acid concentrations to mTORC1, and have an unexpectedly key role in neonates in autophagy induction and thus nutrient homeostasis and viability.