BVES is a novel interactor of ANO5 and regulates myoblast differentiation

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Abstract

Background

Anoctamin 5 (ANO5) is a membrane protein belonging to the TMEM16/Anoctamin family and its deficiency leads to the development of limb girdle muscular dystrophy R12 (LGMDR12). However, little has been known about the interactome of ANO5 and its cellular functions.

Results

In this study, we exploited a proximal labeling approach to identify the interacting proteins of ANO5 in C2C12 myoblasts stably expressing ANO5 tagged with BioID2. Mass spectrometry identified 41 unique proteins including BVES and POPDC3 specifically from ANO5-BioID2 samples, but not from BioID2 fused with ANO6 or MG53. The interaction between ANO5 and BVES was further confirmed by co-immunoprecipitation (Co-IP), and the N-terminus of ANO5 mediated the interaction with the C-terminus of BVES. ANO5 and BVES were co-localized in muscle cells and enriched at the endoplasmic reticulum (ER) membrane. Genome editing-mediated ANO5 or BVES disruption significantly suppressed C2C12 myoblast differentiation with little impact on proliferation.

Conclusions

Taken together, these data suggest that BVES is a novel interacting protein of ANO5, involved in regulation of muscle differentiation.

Supplementary Information

The online version contains supplementary material available at 10.1186/s13578-021-00735-w.

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Most cited references 41

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Programmable editing of a target base in genomic DNA without double-stranded DNA cleavage

Alexis Komor, Yongjoo Kim, Michael Packer … (2016)

Current genome-editing technologies introduce double-stranded (ds) DNA breaks at a target locus as the first step to gene correction. 1,2 Although most genetic diseases arise from point mutations, current approaches to point mutation correction are inefficient and typically induce an abundance of random insertions and deletions (indels) at the target locus from the cellular response to dsDNA breaks. 1,2 Here we report the development of base editing, a new approach to genome editing that enables the direct, irreversible conversion of one target DNA base into another in a programmable manner, without requiring dsDNA backbone cleavage or a donor template. We engineered fusions of CRISPR/Cas9 and a cytidine deaminase enzyme that retain the ability to be programmed with a guide RNA, do not induce dsDNA breaks, and mediate the direct conversion of cytidine to uridine, thereby effecting a C→T (or G→A) substitution. The resulting “base editors” convert cytidines within a window of approximately five nucleotides (nt), and can efficiently correct a variety of point mutations relevant to human disease. In four transformed human and murine cell lines, second- and third-generation base editors that fuse uracil glycosylase inhibitor (UGI), and that use a Cas9 nickase targeting the non-edited strand, manipulate the cellular DNA repair response to favor desired base-editing outcomes, resulting in permanent correction of ∼15-75% of total cellular DNA with minimal (typically ≤ 1%) indel formation. Base editing expands the scope and efficiency of genome editing of point mutations.

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Calcium-dependent phospholipid scramblase activity of TMEM16 protein family members.

Jun Suzuki, Toshihiro Fujii, Takeshi Imao … (2013)

TMEM16A and 16B work as Cl(-) channel, whereas 16F works as phospholipid scramblase. The function of other TMEM16 members is unknown. Using TMEM16F(-/-) cells, TMEM16C, 16D, 16F, 16G, and 16J were shown to be lipid scramblases. Some TMEM16 members are divided into two Cl(-) channels and five lipid scramblases. Learning the biochemical function ofTMEM16family members is essential to understand their physiological role. Asymmetrical distribution of phospholipids between the inner and outer plasma membrane leaflets is disrupted in various biological processes. We recently identified TMEM16F, an eight-transmembrane protein, as a Ca(2+)-dependent phospholipid scramblase that exposes phosphatidylserine (PS) to the cell surface. In this study, we established a mouse lymphocyte cell line with a floxed allele in the TMEM16F gene. When TMEM16F was deleted, these cells failed to expose PS in response to Ca(2+) ionophore, but PS exposure was elicited by Fas ligand treatment. We expressed other TMEM16 proteins in the TMEM16F(-/-) cells and found that not only TMEM16F, but also 16C, 16D, 16G, and 16J work as lipid scramblases with different preference to lipid substrates. On the other hand, a patch clamp analysis in 293T cells indicated that TMEM16A and 16B, but not other family members, acted as Ca(2+)-dependent Cl(-) channels. These results indicated that among 10 TMEM16 family members, 7 members could be divided into two subfamilies, Ca(2+)-dependent Cl(-) channels (16A and 16B) and Ca(2+)-dependent lipid scramblases (16C, 16D, 16F, 16G, and 16J).

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Autophagy as a new therapeutic target in Duchenne muscular dystrophy

C De Palma, F Morisi, S Cheli … (2012)

A resolutive therapy for Duchene muscular dystrophy, a severe degenerative disease of the skeletal muscle, is still lacking. Because autophagy has been shown to be crucial in clearing dysfunctional organelles and in preventing tissue damage, we investigated its pathogenic role and its suitability as a target for new therapeutic interventions in Duchenne muscular dystrophy (DMD). Here we demonstrate that autophagy is severely impaired in muscles from patients affected by DMD and mdx mice, a model of the disease, with accumulation of damaged organelles. The defect in autophagy was accompanied by persistent activation via phosphorylation of Akt, mammalian target of rapamycin (mTOR) and of the autophagy-inhibiting pathways dependent on them, including the translation-initiation factor 4E-binding protein 1 and the ribosomal protein S6, and downregulation of the autophagy-inducing genes LC3, Atg12, Gabarapl1 and Bnip3. The defective autophagy was rescued in mdx mice by long-term exposure to a low-protein diet. The treatment led to normalisation of Akt and mTOR signalling; it also reduced significantly muscle inflammation, fibrosis and myofibre damage, leading to recovery of muscle function. This study highlights novel pathogenic aspects of DMD and suggests autophagy as a new effective therapeutic target. The treatment we propose can be safely applied and immediately tested for efficacy in humans.

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Author and article information

Contributors

Renzhi Han:

ORCID: http://orcid.org/0000-0002-8202-9186

renzhi.han@osumc.edu

Journal

Journal ID (nlm-ta): Cell Biosci

Journal ID (iso-abbrev): Cell Biosci

Title: Cell & Bioscience

Publisher: BioMed Central (London )

ISSN (Electronic): 2045-3701

Publication date (Electronic): 28 December 2021

Publication date PMC-release: 28 December 2021

Publication date Collection: 2021

Volume: 11

Electronic Location Identifier: 222

Affiliations

[1 ]GRID grid.412332.5, ISNI 0000 0001 1545 0811, Division of Cardiac Surgery, Department of Surgery, Davis Heart and Lung Research Institute, , The Ohio State University Wexner Medical Center, ; Columbus, OH 43210 USA

[2 ]GRID grid.216417.7, ISNI 0000 0001 0379 7164, Department of Pediatrics, The Third Xiangya Hospital, , Central South University, ; Changsha, China

Author information

Renzhi Han http://orcid.org/0000-0002-8202-9186

Article

Publisher ID: 735

DOI: 10.1186/s13578-021-00735-w

PMC ID: 8715634

PubMed ID: 34963485

SO-VID: cfdfbd62-32d6-4909-afdd-3c0004c913f2

License:

Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/. The Creative Commons Public Domain Dedication waiver ( http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated in a credit line to the data.

History

Date received : 28 October 2021

Date accepted : 17 December 2021

Funding

Funded by: FundRef http://dx.doi.org/10.13039/100000050, National Heart, Lung, and Blood Institute;

Award ID: R01HL116546

Award ID: R01HL159900

Award Recipient : Renzhi Han

Funded by: FundRef http://dx.doi.org/10.13039/100000069, National Institute of Arthritis and Musculoskeletal and Skin Diseases;

Award ID: R01AR070752

Award Recipient : Renzhi Han

Funded by: FundRef http://dx.doi.org/10.13039/100005693, Parent Project Muscular Dystrophy;

Custom metadata

ScienceOpen disciplines: Cell biology

Keywords: ano5,bioid2,bves,muscle differentiation,muscular dystrophy,proximity labeling

Data availability:

ScienceOpen disciplines: Cell biology

Keywords: ano5, bioid2, bves, muscle differentiation, muscular dystrophy, proximity labeling

BVES is a novel interactor of ANO5 and regulates myoblast differentiation

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Abstract

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Claudins

Most cited references 41

Programmable editing of a target base in genomic DNA without double-stranded DNA cleavage

Calcium-dependent phospholipid scramblase activity of TMEM16 protein family members.

Autophagy as a new therapeutic target in Duchenne muscular dystrophy

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