The DOI matches its Crossref record; 21 of the 21 references it cites were found in a registry or an index.
The functional universe of membrane contact sites
Open accessAbstract
Organelles compartmentalize eukaryotic cells, enhancing their ability to respond to environmental and developmental changes. One way in which organelles communicate and integrate their activities is by forming close contacts, often called ‘membrane contact sites’ (MCSs). Interest in MCSs has grown dramatically in the past decade as it is has become clear that they are ubiquitous and have a much broader range of critical roles in cells than was initially thought. Indeed, functions for MCSs in intracellular signalling (particularly calcium signalling, reactive oxygen species signalling and lipid signalling), autophagy, lipid metabolism, membrane dynamics, cellular stress responses and organelle trafficking and biogenesis have now been reported. Although organelles compartmentalize eukaryotic cells, they can communicate and integrate their activities by connecting at membrane contact sites (MCSs). The roles of MCSs in biology are becoming increasingly clear, with MCSs now known to function in intracellular signalling, lipid metabolism, membrane dynamics, organelle biogenesis and the cellular stress response.
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Cites
Dynamics and functions of lipid droplets
Olzmann, J. A., & Carvalho, P. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0085-z · Cited by 2,740
An ER-Mitochondria Tethering Complex Revealed by a Synthetic Biology Screen
Kornmann, B., Currie, E., Collins, S. R., Schuldiner, M., Nunnari, J., Weissman, J. S., & Walter, P. (2009) · Science · doi:10.1126/science.1175088 · Cited by 1,275
Applying systems-level spectral imaging and analysis to reveal the organelle interactome
Valm, A. M., Cohen, S., Legant, W. R., Melunis, J., Hershberg, U., Wait, E., Cohen, A. R., Davidson, M. W., Betzig, E., & Lippincott-Schwartz, J. (2017) · Nature · doi:10.1038/nature22369 · Cited by 1,113
An Actin-Dependent Step in Mitochondrial Fission Mediated by the ER-Associated Formin INF2
Korobova, F., Ramabhadran, V., & Higgs, H. N. (2013) · Science · doi:10.1126/science.1228360 · Cited by 817
The mammalian ULK1 complex and autophagy initiation
Zachari, M., & Ganley, I. G. (2017) · Essays in Biochemistry · doi:10.1042/ebc20170021 · Cited by 789
ER-mitochondria contacts couple mtDNA synthesis with mitochondrial division in human cells
Lewis, S. C., Uchiyama, L. F., & Nunnari, J. (2016) · Science · doi:10.1126/science.aaf5549 · Cited by 673
Upregulated function of mitochondria‐associated ER membranes in Alzheimer disease
Area‐Gomez, E., del Carmen Lara Castillo, M., Tambini, M. D., Guardia‐Laguarta, C., de Groof, A. J. C., Madra, M., Ikenouchi, J., Umeda, M., Bird, T. D., Sturley, S. L., et al. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.202 · Cited by 638
Nguyen, T. B., Louie, S. M., Daniele, J. R., Tran, Q., Dillin, A., Zoncu, R., Nomura, D. K., & Olzmann, J. A. (2017) · Developmental Cell · doi:10.1016/j.devcel.2017.06.003 · Cited by 610
Multiple dynamin family members collaborate to drive mitochondrial division
Lee, J. E., Westrate, L. M., Wu, H., Page, C., & Voeltz, G. K. (2016) · Nature · doi:10.1038/nature20555 · Cited by 512
Tubbs, E., Theurey, P., Vial, G., Bendridi, N., Bravard, A., Chauvin, M.-A., Ji-Cao, J., Zoulim, F., Bartosch, B., Ovize, M., et al. (2014) · Diabetes · doi:10.2337/db13-1751 · Cited by 411
Cooperative and independent roles of the Drp1 adaptors Mff, MiD49 and MiD51 in mitochondrial fission
Osellame, L. D., Singh, A. P., Stroud, D. A., Palmer, C. S., Stojanovski, D., Ramachandran, R., & Ryan, M. T. (2016) · Journal of Cell Science · doi:10.1242/jcs.185165 · Cited by 336
Murley, A., Lackner, L. L., Osman, C., West, M., Voeltz, G. K., Walter, P., & Nunnari, J. (2013) · eLife · doi:10.7554/elife.00422 · Cited by 326
Shai, N., Yifrach, E., van Roermund, C. W. T., Cohen, N., Bibi, C., IJlst, L., Cavellini, L., Meurisse, J., Schuster, R., Zada, L., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-03957-8 · Cited by 320
Understanding phosphoinositides: rare, dynamic, and essential membrane phospholipids
Dickson, E. J., & Hille, B. (2019) · Biochemical Journal · doi:10.1042/bcj20180022 · Cited by 254
PDK4 augments ER-mitochondria contact to dampen skeletal muscle insulin signaling during obesity
Thoudam, T., Ha, C.-M., Leem, J., Chanda, D., Park, J.-S., Kim, H.-J., Jeon, J.-H., Choi, Y.-K., Liangpunsakul, S., Huh, Y. H., et al. (2019) · Diabetes · doi:10.2337/db18-0363 · Cited by 207
Constriction of the mitochondrial inner compartment is a priming event for mitochondrial division
Cho, B., Cho, H. M., Jo, Y., Kim, H. D., Song, M., Moon, C., Kim, H., Kim, K., Sesaki, H., Rhyu, I. J., et al. (2017) · Nature Communications · doi:10.1038/ncomms15754 · Cited by 179
Power Grid Protection of the Muscle Mitochondrial Reticulum
Glancy, B., Hartnell, L. M., Combs, C. A., Femnou, A., Sun, J., Murphy, E., Subramaniam, S., & Balaban, R. S. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.03.063 · Cited by 172
Trans-mitochondrial coordination of cristae at regulated membrane junctions
Picard, M., McManus, M. J., Csordás, G., Várnai, P., Dorn II, G. W., Williams, D., Hajnóczky, G., & Wallace, D. C. (2015) · Nature Communications · doi:10.1038/ncomms7259 · Cited by 166
Structure–Function Insights into Direct Lipid Transfer between Membranes by Mmm1–Mdm12 of ERMES
Kawano, S., Tamura, Y., Kojima, R., Bala, S., Asai, E., Michel, A. H., Kornmann, B., Riezman, I., Riezman, H., Sakae, Y., et al. (2018) · Journal of Cell Biology · doi:10.1083/jcb.201704119 · Cited by 148
Gutiérrez, T., & Simmen, T. (2018) · Cell Calcium · doi:10.1016/j.ceca.2017.05.015 · Cited by 104
The ins and outs of iron: Escorting iron through the mammalian cytosol
Philpott, C. C., & Jadhav, S. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.10.411 · Cited by 100
Cited by
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Posor, Y., Jang, W., & Haucke, V. (2022) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-022-00490-x · Cited by 469
Lipid droplet contact sites in health and disease
Herker, E., Vieyres, G., Beller, M., Krahmer, N., & Bohnert, M. (2021) · Trends in Cell Biology · doi:10.1016/j.tcb.2021.01.004 · Cited by 174
Molecular basis of accessible plasma membrane cholesterol recognition by the GRAM domain of GRAMD1b
Ercan, B., Naito, T., Koh, D. H. Z., Dharmawan, D., & Saheki, Y. (2021) · The EMBO Journal · doi:10.15252/embj.2020106524 · Cited by 132
Castro, I. G., Shortill, S. P., Dziurdzik, S. K., Cadou, A., Ganesan, S., Valenti, R., David, Y., Davey, M., Mattes, C., Thomas, F. B., et al. (2022) · eLife · doi:10.7554/elife.74602 · Cited by 60
Metadata
- Authors
- Prinz, W. A., Toulmay, A., & Balla, T.
- Venue
- Nature Reviews Molecular Cell Biology
- Published
- 2019-11-15
- Volume
- 21
- Issue
- 1
- Pages
- 7-24
- ISSN
- 1471-0072 (ISSN-L)
- 1471-0080
- OpenAlex
- W2987979134
- Cited by
- 726
- References
- 21
- FWCI
- 7.35
- Type
- journal article
- Language
- en
- Open access
- green
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