S
Sandra L. Schmid
Researcher at University of Texas Southwestern Medical Center
Publications - 209
Citations - 32222
Sandra L. Schmid is an academic researcher from University of Texas Southwestern Medical Center. The author has contributed to research in topics: Endocytosis & Dynamin. The author has an hindex of 89, co-authored 209 publications receiving 30096 citations. Previous affiliations of Sandra L. Schmid include University of British Columbia & Stanford University.
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Journal ArticleDOI
Crosstalk between Akt/GSK3β signaling and dynamin-1 regulates clathrin-mediated endocytosis.
Carlos R. Reis,Ping Hung Chen,Saipraveen Srinivasan,François Aguet,Marcel Mettlen,Sandra L. Schmid +5 more
TL;DR: It is shown that nascent endocytic vesicles formed in mutant cells displaying rapid, dysregulated CME are defective in early endosomal trafficking, maturation and acidification, confirming the importance of this “checkpoint.”
Journal ArticleDOI
Expression of Mutant Dynamin Inhibits Toxicity and Transport of Endocytosed Ricin to the Golgi Apparatus
TL;DR: Data demonstrate that although ricin is internalized by clathrin-independent endocytosis in cells expressing mutant dynamin, there is a strong and apparently selective inhibition of ricin transport to the Golgi apparatus.
Journal ArticleDOI
Endocytic accessory proteins are functionally distinguished by their differential effects on the maturation of clathrin-coated pits
Marcel Mettlen,Miriam Carolin Stoeber,Miriam Carolin Stoeber,Dinah Loerke,Costin N. Antonescu,Gaudenz Danuser,Sandra L. Schmid +6 more
TL;DR: The results support the idea that a subset of accessory proteins, which mediate coat assembly, membrane curvature, and cargo selection, can provide input into an endocytic restriction point/checkpoint mechanism that monitors CCP maturation.
Book ChapterDOI
Tightly regulated and inducible expression of dominant interfering dynamin mutant in stably transformed HeLa cells.
TL;DR: This chapter describes the successful use of the tetracycline-inducible expression system for the analysis of dynamin's function in receptor-mediated endocytosis and offers some practical advice for its establishment.
Journal ArticleDOI
Ubiquitously Expressed Dynamin-II Has a Higher Intrinsic GTPase Activity and a Greater Propensity for Self-assembly Than Neuronal Dynamin-I
TL;DR: Results are consistent with the hypothesis that self-assembly is a major regulator of dynamin GTPase activity and that the intrinsic rate of GTP hydrolysis reflects a dynamic, GTP-dependent equilibrium of assembly and disassembly.