Marta Campiglio

Group/personal information:

AG: Campiglio
Group leader: Marta Campiglio
Location: Schöpfstr. 41/UG floor, office 68
Phone: +43 (0) 512 9003 70841
ORCID: 0000-0002-9629-2073
Twitter: @CampiglioLab

Scientific interests:

Our main interest is skeletal muscle excitation-contraction (EC) coupling, which depends on the physical interaction of the voltage sensor, the voltage-gated calcium channel CaV1.1 on the transverse tubule membrane, and the calcium release channel, the RyR1 (Ryanodine receptor 1) on the sarcoplasmic reticulum. The mechanism of this interaction is still elusive and recently an adaptor protein, STAC3, was identified as essential in this process. Our research efforts aim at advancing the understanding the role of the interactions established by the voltage sensor CaV1.1, the adaptor protein STAC3 and the calcium release channel RyR1.

Current research topics:

  • Dissecting the role of multiple STAC3/CaV1.1 interactions in skeletal muscle EC coupling
  • Understanding the molecular mechanisms of skeletal muscle pathologies

Main methodologies:

  • Skeletal muscle cell culture
  • Patch-clamp and fluorescent calcium recordings
  • CRIPR/Cas9 gene editing

Current lab members:

PhD students:

Wiestke Tuinte
Enikö Török

Technical support:

Maria Kharitonova

Funding sources:

Fonds zur Förderung Wissenschaftlicher Forschung (FWF)
P33776, DOC30, DOC128


Prof. Filip Van Petegem (University of British Columbia, Canada)
Prof. Daniel Minor, Jr. (University of California San Francisco, USA)
Prof. Manu Ben-Johny (Columbia University, USA)

Selected publications:

  1. El Ghaleb, Y., Ortner, N. J., Posch, W., Fernandez-Quintero, M. L., Tuinte, W. E., Monteleone, S., . . . Campiglio, M. (2022). Calcium current modulation by the gamma1 subunit depends on alternative splicing of CaV1.1. J Gen Physiol, 154(9). doi:10.1085/jgp.202113028
  2. El Ghaleb, Y., P. E. Schneeberger, M. L. Fernandez-Quintero, S. M. Geisler, S. Pelizzari, A. M. Polstra, J. M. van Hagen, J. Denecke, M. Campiglio, K. R. Liedl, C. A. Stevens, R. E. Person, S. Rentas, E. D. Marsh, L. K. Conlin, P. Tuluc, K. Kutsche, and B. E. Flucher. 2021. CACNA1I gain-of-function mutations differentially affect channel gating and cause neurodevelopmental disorders. Brain. doi: 10.1093/brain/awab101.
  3. Rufenach, B., D. Christy, B. E. Flucher, J. M. Bui, J. Gsponer, M. Campiglio, and F. Van Petegem. 2020. Multiple Sequence Variants in STAC3 Affect Interactions with CaV1.1 and Excitation-Contraction Coupling. Structure. 28(8):922-932 e925, doi: 10.1016/j.str.2020.05.005.
  4. Flucher, B. E., and M. Campiglio. 2019. STAC proteins: The missing link in skeletal muscle EC coupling and new regulators of calcium channel function. Biochim Biophys Acta Mol Cell Res. 1866(7):1101-1110, doi: 10.1016/j.bbamcr.2018.12.004.
  5. Campiglio, M., M. M. Kaplan, and B. E. Flucher. 2018. STAC3 incorporation into skeletal muscle triads occurs independent of the dihydropyridine receptor. J Cell Physiol. 233(12):9045-9051, doi: 10.1002/jcp.26767.
  6. Campiglio, M., P. Coste de Bagneaux, N. J. Ortner, P. Tuluc, F. Van Petegem, and B. E. Flucher. 2018. STAC proteins associate to the IQ domain of CaV1.2 and inhibit calcium-dependent inactivation. Proc Natl Acad Sci U S A. 115(6):1376-1381, doi: 10.1073/pnas.1715997115.
  7. Wong King Yuen, S. M., M. Campiglio, C. C. Tung, B. E. Flucher, and F. Van Petegem. 2017. Structural insights into binding of STAC proteins to voltage-gated calcium channels. Proc Natl Acad Sci U S A. 114(45):E9520-E9528, doi: 10.1073/pnas.1708852114.
  8. Campiglio, M., and B. E. Flucher. 2017. STAC3 stably interacts through its C1 domain with CaV1.1 in skeletal muscle triads. Sci Rep. 7:41003, doi: 10.1038/srep41003.
  9. Campiglio, M., and B. E. Flucher. 2015. The role of auxiliary subunits for the functional diversity of voltage-gated calcium channels. J Cell Physiol. 230(9):2019-2031, doi: 10.1002/jcp.24998.
  10. Campiglio, M., V. Di Biase, P. Tuluc, and B. E. Flucher. 2013. Stable incorporation versus dynamic exchange of beta subunits in a native Ca2+ channel complex. J Cell Sci. 126(Pt 9):2092-2101, doi: 10.1242/jcs.jcs124537.

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