EHD1 mediates vesicle trafficking required for normal muscle growth and transverse tubule development
Open accessAbstract
EHD proteins have been implicated in intracellular trafficking, especially endocytic recycling, where they mediate receptor and lipid recycling back to the plasma membrane. Additionally, EHDs help regulate cytoskeletal reorganization and induce tubule formation. It was previously shown that EHD proteins bind directly to the C2 domains in myoferlin, a protein that regulates myoblast fusion. Loss of myoferlin impairs normal myoblast fusion leading to smaller muscles in vivo but the intracellular pathways perturbed by loss of myoferlin function are not well known. We now characterized muscle development in EHD1-null mice. EHD1-null myoblasts display defective receptor recycling and mislocalization of key muscle proteins, including caveolin-3 and Fer1L5, a related ferlin protein homologous to myoferlin. Additionally, EHD1-null myoblast fusion is reduced. We found that loss of EHD1 leads to smaller muscles and myofibers in vivo. In wildtype skeletal muscle EHD1 localizes to the transverse tubule (T-tubule), and loss of EHD1 results in overgrowth of T-tubules with excess vesicle accumulation in skeletal muscle. We provide evidence that tubule formation in myoblasts relies on a functional EHD1 ATPase domain. Moreover, we extended our studies to show EHD1 regulates BIN1 induced tubule formation. These data, taken together and with the known interaction between EHD and ferlin proteins, suggests that the EHD proteins coordinate growth and development likely through mediating vesicle recycling and the ability to reorganize the cytoskeleton.
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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 [44]
The Results section, “EHD1 regulates BIN1 tubule formation” (page not supplied), shows that EHD1 affects BIN1-induced tubules. The Results on defective endosomal trafficking show impaired recycling in EHD1-null myoblasts, and the Introduction names MICAL-L1 as an EHD-interacting protein. Our copy does not establish that EHD proteins recycle vesicles together with Rab8a or Rab11-FIP2; it discusses Rab11, but not Rab11-FIP2. (LLM, conf=0.88)
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- Authors
- Posey, A. D., Swanson, K. E., Alvarez, M. G., Krishnan, S., Earley, J. U., Band, H., Pytel, P., McNally, E. M., & Demonbreun, A. R.
- Affiliations
- University of Chicago (US)
- University of Nebraska Medical Center (US)
- Corresponding author
- Demonbreun, Alexis R.
- ORCID
- Venue
- Developmental Biology
- Publisher
- Elsevier BV
- Published
- 2014-03
- Volume
- 387
- Issue
- 2
- Pages
- 179-190
- ISSN
- 0012-1606 (ISSN-L)
- PMC
- PMC3987670
- OpenAlex
- W2466426764
- Cited by
- 52
- References
- 51
- Citations by year
- 2026: 5 · 2025: 2 · 2024: 3 · 2022: 2 · 2021: 7 · 2020: 6 · 2019: 5 · 2018: 2 · 2017: 3 · 2016: 6 · 2015: 8 · 2014: 3
- FWCI
- 2.52
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Developmental Biology (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- NIH (NS047726)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Caveolin-1 and cellular processes
- Keywords
- EHD1, vesicle trafficking, skeletal muscle development, myoblast fusion, myoferlin, receptor recycling, caveolin-3, BIN1, cytoskeletal remodeling
- MeSH terms
- Animals, Cytoskeleton, Membrane Proteins, Muscle Proteins, Nerve Tissue Proteins, Sarcolemma, Mice, Knockout, Protein Transport, Muscle Development, Tumor Suppressor Proteins, Myoblasts, Vesicular Transport Proteins, Adaptor Proteins, Signal Transducing, Caveolin 3, Mice, Quadriceps Muscle
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