Research progress on biological function of mitochondria-associated endoplasmic reticulum membranes and its role in related diseases

doi:10.3877/cma.j.issn.2095-655X.2022.04.014

Abstract

Abstract:

" Mitochondrial-associated endoplasmic reticulum membranes (MAMs)" refer to the region where the endoplasmic reticulum and the outer membrane of the mitochondria come into contact. MAMs contain carrier proteins, channel proteins, and membrane proteins. MAMs can take part in a wide range of biological processes, such as mitophagy, Ca²⁺ release, inflammatory response, lipid metabolism, and neoangiogenesis. They can also affect the disease development, such as like cardiovascular disease, diabetes, and cancer. This essay′s primary objective is to summarize the numerous biological functions of MAMs and how those functions relate to various diseases.

Key words: Mitochondria-associated endoplasmic reticulum membranes, Mitophagy, Ca²⁺ release, FUN 14 domain containing 1, Neoangiogenesis

Lu Yu, Yonghua Li. Research progress on biological function of mitochondria-associated endoplasmic reticulum membranes and its role in related diseases[J]. Chinese Journal of Diagnostics(Electronic Edition), 2022, 10(04): 284-288.

/ / Recommend

Add to citation manager EndNote|Ris|BibTeX

URL: https://zhzdxdzzz.cma-cmc.com.cn/EN/10.3877/cma.j.issn.2095-655X.2022.04.014

https://zhzdxdzzz.cma-cmc.com.cn/EN/Y2022/V10/I04/284

References 37

[1]	Poston CN, Krishnan SC, Bazemore-Walker CR.In-depth proteomic analysis of mammalian mitochondria-associated membranes(MAM)[J]．J Proteomics，2013(79):219-230.DOI：10.1016/j.jprot.2012.12.018.
[2]	Barazzuol L, Giamogante F, Calì T．Mitochondria associated membranes(MAMs)：architecture and physiopathological role[J]．Cell Calcium，2021(94):102343.DOI：10.1016/j.ceca.2020.102343.
[3]	Yang JY, Yang WY. Bit-by-bit autophagic removal of parkin-labelled mitochondria[J]．Nat Commun，2013(4):2428.DOI：10.1038/ncomms3428.
[4]	Kornmann B, Currie E, Collins SR, et al. An ER-mitochondria tethering complex revealed by a synthetic biology screen[J]．Science，2009，325(5939):477-481.DOI：10.1126/science.1175088.
[5]	Gelmetti V, De Rosa P, Torosantucci L，et al.PINK1 and BECN1 relocalize at mitochondria-associated membranes during mitophagy and promote ER-mitochondria tethering and autophagosome formation[J]．Autophagy，2017，13(4):654-669.DOI：10.1080/15548627.2016.1277309.
[6]	Pickrell AM, Youle RJ.The roles of PINK1，parkin，and mitochondrial fidelity in Parkinson's disease[J]．Neuron，2015，85(2):257-273.DOI：10.1016/j.neuron.2014.12.007.
[7]	Birgisdottir ÅB, Lamark T, Johansen T．The LIR motif-crucial for selective autophagy[J]．J Cell Sci，2013，126(Pt 15):3237-3247.DOI：10.1242/jcs.126128.
[8]	Wu W, Lin C, Wu K, et al. FUNDC1 regulates mitochondrial dynamics at the ER-mitochondrial contact site under hypoxic conditions[J]．EMBO J，2016，35(13):1368-1384.DOI：10.15252/embj.201593102.
[9]	Li W, Zhang X, Zhuang H，et al.MicroRNA-137 is a novel hypoxia-responsive microRNA that inhibits mitophagy via regulation of two mitophagy receptors FUNDC1 and NIX[J]．J Biol Chem，2014，289(15):10691-10701.DOI：10.1074/jbc.M113.537050.
[10]	Mercer TJ, Gubas A, Tooze SA.A molecular perspective of mammalian autophagosome biogenesis[J]．J Biol Chem，2018，293(15):5386-5395.DOI：10.1074/jbc.R117.810366.
[11]	de Brito OM, Scorrano L．Mitofusin 2 tethers endoplasmic reticulum to mitochondria[J]．Nature，2008，456(7222):605-610.DOI：10.1038/nature07534.
[12]	Missiroli S, Patergnani S, Caroccia N，et al.Mitochondria-associated membranes (MAMs) and inflammation[J]．Cell Death Dis，2018，9(3):329.DOI：10.1038/s41419-017-0027-2.
[13]	Zhou R, Yazdi AS, Menu P，et al.A role for mitochondria in NLRP3 inflammasome activation[J]．Nature，2011，469(7329):221-225.DOI：10.1038/nature09663.
[14]	Qu C, Li Y, Li Y，et al.Full-length MAVS，a mitochondrial antiviral-signaling protein，inhibits hepatitis E virus replication，requiring JAK-STAT signaling[J]．Arch Virol，2022，167(5):1293-1300.DOI：10.1007/s00705-022-05415-9.
[15]	Bender S, Reuter A, Eberle F，et al.Activation of type Ⅰ and Ⅲ interferon response by mitochondrial and peroxisomal MAVS and inhibition by hepatitis C virus[J]．PLoS Pathog，2015，11(11):e1005264.DOI：10.1371/journal.ppat.1005264.
[16]	Marquette A, Leborgne C, Schartner V，et al.Peptides derived from the C-terminal domain of HIV-1 viral protein R in lipid bilayers：structure，membrane positioning and gene delivery[J]．Biochim Biophys Acta Biomembr，2020，1862(2):183149.DOI：10.1016/j.bbamem.2019.183149.
[17]	Petrungaro C, Kornmann B．Lipid exchange at ER-mitochondria contact sites：a puzzle falling into place with quite a few pieces missing[J]．Curr Opin Cell Biol，2019(57):71-76.DOI：10.1016/j.ceb.2018.11.005.
[18]	Sohn M, Korzeniowski M, Zewe JP，et al.PI(4，5)P2 controls plasma membrane PI4P and PS levels via ORP5/8 recruitment to ER-PM contact sites[J]．J Cell Biol，2018，217(5):1797-1813.DOI：10.1083/jcb.201710095.
[19]	Wang C, Dai X, Wu S，et al.FUNDC1-dependent mitochondria-associated endoplasmic reticulum membranes are involved in angiogenesis and neoangiogenesis[J]．Nat Commun，2021，12(1):2616.DOI：10.1038/s41467-021-22771-3.
[20]	Silva-Palacios A, Zazueta C, Pedraza-Chaverri J．ER membranes associated with mitochondria：possible therapeutic targets in heart-associated diseases[J]．Pharmacol Res，2020(156):104758.DOI：10.1016/j.phrs.2020.104758.
[21]	Tan Y, Zhang Z, Zheng C，et al.Mechanisms of diabetic cardiomyopathy and potential therapeutic strategies：preclinical and clinical evidence[J]．Nat Rev Cardiol，2020，17(9):585-607.DOI：10.1038/s41569-020-0339-2.
[22]	Wu S, Lu Q, Ding Y，et al.Hyperglycemia-driven inhibition of AMP-activated protein kinase α2 induces diabetic cardiomyopathy by promoting mitochondria-associated endoplasmic reticulum membranes in vivo[J]．Circulation，2019，139(16):1913-1936.DOI：10.1161/CIRCULATIONAHA.118.033552.
[23]	Wu S, Lu Q, Wang Q，et al.Binding of FUN14 domain containing 1 with inositol 1，4，5-trisphosphate receptor in mitochondria-associated endoplasmic reticulum membranes maintains mitochondrial dynamics and function in hearts in vivo[J]．Circulation，2017，136(23):2248-2266.DOI：10.1161/CIRCULATIONAHA.117.030235.
[24]	Eizirik DL, Pasquali L, Cnop M．Pancreatic β-cells in type 1 and type 2 diabetes mellitus：different pathways to failure[J]．Nat Rev Endocrinol，2020，16(7):349-362.DOI：10.1038/s41574-020-0355-7.
[25]	Rieusset J．Contribution of mitochondria and endoplasmic reticulum dysfunction in insulin resistance：distinct or interrelated roles？[J]．Diabetes Metab，2015，41(5):358-368.DOI：10.1016/j.diabet.2015.02.006.
[26]	Chen Y, Chen J, Zhang C，et al.Deficiency in the short-chain acyl-CoA dehydrogenase protects mice against diet-induced obesity and insulin resistance[J]．FASEB J，2019，33(12):13722-13733.DOI：10.1096/fj.201901474RR.
[27]	Siasos G, Paschou SA, Tousoulis D．Mitochondria and diabetes[J]．Ann Transl Med，2020，8(6):262.DOI：10.21037/atm.2020.03.15.
[28]	Tubbs E, Chanon S, Robert M，et al.Disruption of mitochondria-associated endoplasmic reticulum membrane (MAM) integrity contributes to muscle insulin resistance in mice and humans[J]．Diabetes，2018，67(4):636-650.DOI：10.2337/db17-0316.
[29]	Rieusset J．Role of endoplasmic reticulum-mitochondria communication in type 2 diabetes[J]．Adv Exp Med Biol，2017(997):171-186.DOI：10.1007/978-981-10-4567-7_13.
[30]	Wu H, Wang Y, Li W，et al.Deficiency of mitophagy receptor FUNDC1 impairs mitochondrial quality and aggravates dietary-induced obesity and metabolic syndrome[J]．Autophagy，2019，15(11):1882-1898.DOI：10.1080/15548627.2019.1596482.
[31]	Kharitonenkov A, DiMarchi R．Fibroblast growth factor 21 night watch：advances and uncertainties in the field[J]．J Intern Med，2017，281(3):233-246.DOI：10.1111/joim.12580.
[32]	Jimenez V, Jambrina C, Casana E，et al.FGF21 gene therapy as treatment for obesity and insulin resistance[J]．EMBO Mol Med，2018，10(8):e8791.DOI：10.15252/emmm.201708791.
[33]	Parys JB, Bultynck G, Vervliet T．IP(3) receptor biology and endoplasmic reticulum calcium dynamics in cancer[J]．Prog Mol Subcell Biol，2021(59):215-237.DOI：10.1007/978-3-030-67696-4_11.
[34]	Xu K, Chen G, Li X，et al.MFN2 suppresses cancer progression through inhibition of mTORC2/Akt signaling[J]．Sci Rep，2017(7):41718.DOI：10.1038/srep41718.
[35]	Rimessi A, Pedriali G, Vezzani B，et al.Interorganellar calcium signaling in the regulation of cell metabolism：a cancer perspective[J]．Semin Cell Dev Biol，2020(98):167-180.DOI：10.1016/j.semcdb.2019.05.015.
[36]	Rong YP, Bultynck G, Aromolaran AS，et al.The BH4 domain of Bcl-2 inhibits ER calcium release and apoptosis by binding the regulatory and coupling domain of the IP3 receptor[J]．Proc Natl Acad Sci U S A，2009，106(34):14397-14402.DOI：10.1073/pnas.0907555106.
[37]	Wu L, Zhang D, Zhou L, et al. FUN14 domain-containing 1 promotes breast cancer proliferation and migration by activating calcium-NFATC1-BMI1 axis[J]．EBioMedicine，2019(41):384-394.DOI：10.1016/j.ebiom.2019.02.032.

Please choose a citation manager

Content to export