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Robert G. Parton
Researcher at University of Queensland
Publications - 513
Citations - 66012
Robert G. Parton is an academic researcher from University of Queensland. The author has contributed to research in topics: Caveolae & Endosome. The author has an hindex of 136, co-authored 459 publications receiving 59737 citations. Previous affiliations of Robert G. Parton include University of Adelaide & French Institute of Health and Medical Research.
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Journal ArticleDOI
The multiple faces of caveolae
Robert G. Parton,Kai Simons +1 more
TL;DR: The apparently diverse functions of caveolae, including mechanosensing and lipid regulation, might be linked to their ability to respond to plasma membrane changes, a property that is dependent on their specialized lipid composition and biophysical properties.
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Rab11 regulates recycling through the pericentriolar recycling endosome.
TL;DR: A novel role for rab11 in controlling traffic through the recycling endosome is suggested after functional studies showed that the early steps of uptake and recycling for transferrin were not affected by overexpression of rab11 proteins.
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The small GTPase rab5 functions as a regulatory factor in the early endocytic pathway.
Cecilia Bucci,Robert G. Parton,Ian H. Mather,Henk Stunnenberg,Kai Simons,Bernard Hoflack,Marino Zerial +6 more
TL;DR: It is concluded that rab5 is a rate-limiting component of the machinery regulating the kinetics of membrane traffic in the early endocytic pathway.
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Kidney organoids from human iPS cells contain multiple lineages and model human nephrogenesis
Minoru Takasato,Minoru Takasato,Pei Xuan Er,Han Sheng Chiu,Barbara Maier,Gregory J. Baillie,Charles Ferguson,Robert G. Parton,Ernst J. Wolvetang,Matthias S Roost,Susana M. Chuva de Sousa Lopes,Melissa H. Little,Melissa H. Little,Melissa H. Little +13 more
TL;DR: The developmental mechanism regulating the preferential induction of collecting duct versus kidney mesenchyme progenitors is identified and kidney organoids that contain nephrons associated with a collecting duct network surrounded by renal interstitium and endothelial cells are generated.
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Localization of low molecular weight GTP binding proteins to exocytic and endocytic compartments.
TL;DR: Findings provide evidence that members of the YPT1/SEC4 subfamily of GTP binding proteins are localized to specific exocytic and endocytic subcompartments in mammalian cells.