EHD proteins: key conductors of endocytic transport
Open accessAbstract
Regulation of endocytic transport is controlled by an elaborate network of proteins. Rab GTP-binding proteins and their effectors have well-defined roles in mediating specific endocytic transport steps, but until recently less was known about the four mammalian dynamin-like C-terminal Eps15 homology domain (EHD) proteins that also regulate endocytic events. In recent years, however, great strides have been made in understanding the structure and function of these unique proteins. Indeed, a growing body of literature addresses EHD protein structure, interactions with binding partners, functions in mammalian cells, and the generation of various new model systems. Accordingly, this is now an opportune time to pause and review the function and mechanisms of action of EHD proteins, and to highlight some of the challenges and future directions for the field.
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EHD proteins regulate BIN1 activity and are required for endocytic vesicle recycling together with Rab8a, Rab11-FIP2 and MICAL-L1.
“EHD proteins regulate BIN1 activity and are required for endocytic vesicle recycling together with Rab8a, Rab11-FIP2 and MICAL-L1 (16,43,44).”
From BIN1 regulates BACE1 intracellular trafficking and amyloid-β production (2016) · cites this paper as [43]
The EHD1 section reports that EHD1 regulates receptor recycling and interacts with Rab11-FIP2; the membrane-binders section identifies MICAL-L1 as an EHD1 partner. The latter section describes Rab8a as a marker of EHD1-decorated tubules, not as a demonstrated partner required for recycling. It also describes EHD1 and BIN1 as potentially cooperating in membrane tubulation, not EHD proteins regulating BIN1 activity. Page numbers are unavailable in our copy. (LLM, conf=0.86)
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Cites
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- Authors
- Naslavsky, N., & Caplan, S.
- Affiliations
- University of Nebraska Medical Center (US)
- Corresponding author
- Caplan, Steve
- Venue
- Trends in Cell Biology
- Publisher
- Elsevier BV
- Published
- 2011-02
- Volume
- 21
- Issue
- 2
- Pages
- 122-131
- ISSN
- 0962-8924 (ISSN-L)
- PMC
- PMC3052690
- OpenAlex
- W1966231010
- Cited by
- 237
- References
- 4
- Citations by year
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- FWCI
- 1.39
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Trends in Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institute of General Medical Sciences (R01GM087455, R01GM074876)
- National Center for Research Resources (P20RR018759)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Caveolin-1 and cellular processes
- Keywords
- endocytic transport, endocytosis, Rab GTPases, protein structure, protein-protein interaction, membrane trafficking
- MeSH terms
- Animals, Biological Transport, Endocytosis, Humans, Vesicular Transport Proteins
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