The Interaction of Epsin and Eps15 with the Clathrin Adaptor AP-2 Is Inhibited by Mitotic Phosphorylation and Enhanced by Stimulation-dependent Dephosphorylation in Nerve Terminals
Open accessAbstract
Clathrin-mediated endocytosis was shown to be arrested in mitosis due to a block in the invagination of clathrin-coated pits. A Xenopus mitotic phosphoprotein, MP90, is very similar to an abundant mammalian nerve terminal protein, epsin, which binds the Eps15 homology (EH) domain of Eps15 and the alpha-adaptin subunit of the clathrin adaptor AP-2. We show here that both rat epsin and Eps15 are mitotic phosphoproteins and that their mitotic phosphorylation inhibits binding to the appendage domain of alpha-adaptin. Both epsin and Eps15, like other cytosolic components of the synaptic vesicle endocytic machinery, undergo constitutive phosphorylation and depolarization-dependent dephosphorylation in nerve terminals. Furthermore, their binding to AP-2 in brain extracts is enhanced by dephosphorylation. Epsin together with Eps15 was proposed to assist the clathrin coat in its dynamic rearrangements during the invagination/fission reactions. Their mitotic phosphorylation may be one of the mechanisms by which the invagination of clathrin-coated pits is blocked in mitosis and their stimulation-dependent dephosphorylation at synapses may contribute to the compensatory burst of endocytosis after a secretory stimulus.
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Epsin1 interacts with other endocytic proteins such as Eps15 and Hip1R, both of which interact either directly or indirectly with membranes and actin.
“However, it is not clear whether Epsin1 is the sole organizer of F-actin at synapses, since it interacts with other endocytic proteins such as Eps15 and Hip1R72,88, both of which interact either directly or indirectly with membranes and actin.”
From Membrane compression by synaptic vesicle exocytosis triggers ultrafast endocytosis (2023) · cites this paper as [88]
The introductory passage identifies epsin as a major binding partner of Eps15, supporting that interaction. It does not address Hip1R or establish that both proteins interact with membranes and actin; the cited paper therefore supports only part of the attributed claim. (LLM, conf=0.86)
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- Authors
- Chen, H., Slepnev, V. I., Di Fiore, P. P., & De Camilli, P.
- Affiliations
- Howard Hughes Medical Institute (US)
- ORCID
- Chen, Hong
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1999-02
- Volume
- 274
- Issue
- 6
- Pages
- 3257-3260
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1994912740
- Cited by
- 138
- References
- 34
- Citations by year
- 2026: 1 · 2025: 2 · 2024: 2 · 2023: 4 · 2022: 2 · 2021: 2 · 2020: 3 · 2019: 1 · 2017: 4 · 2015: 1 · 2014: 6 · 2013: 2 · 2012: 13
- FWCI
- 5.53
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- INFM-OAR (INFN Catania) (submittedVersion, cc-by)
- Funders
- National Cancer Institute (P01CA046128, CA46128)
- National Institute of Neurological Disorders and Stroke (NS36251)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ion Transport and Channel Regulation
- Keywords
- epsin, Eps15, alpha-adaptin, mitotic phosphorylation, dephosphorylation, clathrin-mediated endocytosis, mitosis, presynaptic terminals, synaptic vesicle endocytosis
- MeSH terms
- Animals, Base Sequence, Calcium-Binding Proteins, Carrier Proteins, Cell Line, Endocytosis, Exocytosis, Membrane Proteins, Mitosis, Nerve Endings, Neuropeptides, Phosphoproteins, Phosphorylation, Protein Binding, DNA Primers, Vesicular Transport Proteins, Adaptor Proteins, Vesicular Transport, Adaptor Protein Complex alpha Subunits, Intracellular Signaling Peptides and Proteins, Adaptor Proteins, Signal Transducing, Mice, Rats
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