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Fine-tuning activity-dependent bulk endocytosis via kinases and phosphatases

descriptionPublicationkeyboard_double_arrow_right Article , Other literature type 19 Nov 2021 English Publisher:Rockefeller University PressJournal:Journal of Cell Biology, volume 220 (issn: 0021-9525, eissn: 1540-8140, Copyright policy )Funded by:EC | MIA-Portugal, WT | Determining the role of a...
Authors: Ira Milosevic; Michael A. Cousin;

doi: 10.1083/jcb.202111056

pmid: 34797376

pmc: PMC8610339

handle: 10316/96941 , 20.500.11820/ad4a27bc-5361-4322-aaf3-d5115e2c4656

Fine-tuning activity-dependent bulk endocytosis via kinases and phosphatases

Abstract

The regulation of activity-dependent bulk endocytosis, the dominant mode of membrane retrieval in response to intense neuronal activity, is poorly understood. In this JCB issue, Peng et al. (2021. J. Cell. Biol.https://doi.org/10.1083/jcb.202011028) propose a novel molecular mechanism for the coordination of activity-dependent bulk endocytosis that builds on Minibrain kinase and its presynaptic substrate synaptojanin-1.

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Keywords

Spotlight, Endocytosis, Phosphoric Monoester Hydrolases

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citations
This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Citations provided by BIP!
popularity
This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
BIP!Popularity provided by BIP!
influence
This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Influence provided by BIP!
impulse
This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.
BIP!Impulse provided by BIP!
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