LRRK2 phosphorylation status and kinase activity regulate (macro)autophagy in a Rab8a/Rab10-dependent manner

Autor: Elżbieta Kania, Jaclyn S. Long, David G. McEwan, Kirsten Welkenhuyzen, Rita La Rovere, Tomas Luyten, John Halpin, Evy Lobbestael, Veerle Baekelandt, Geert Bultynck, Kevin M. Ryan, Jan B. Parys

Publikováno v: Cell Death and Disease, Vol 14, Iss 7, Pp 1-14 (2023)

Abstract Mutations in the leucine-rich repeat kinase 2 (LRRK2) gene are the most common genetic cause of Parkinson’s disease (PD), with growing importance also for Crohn’s disease and cancer. LRRK2 is a large and complex protein possessing both G

Externí odkaz: https://doaj.org/article/ac990b44ebe440e7985118a7bf10125c

TRPC3 shapes the ER-mitochondria Ca2+ transfer characterizing tumour-promoting senescence

Autor: Valerio Farfariello, Dmitri V. Gordienko, Lina Mesilmany, Yasmine Touil, Emmanuelle Germain, Ingrid Fliniaux, Emilie Desruelles, Dimitra Gkika, Morad Roudbaraki, George Shapovalov, Lucile Noyer, Mathilde Lebas, Laurent Allart, Nathalie Zienthal-Gelus, Oksana Iamshanova, Franck Bonardi, Martin Figeac, William Laine, Jerome Kluza, Philippe Marchetti, Bruno Quesnel, Daniel Metzger, David Bernard, Jan B. Parys, Loïc Lemonnier, Natalia Prevarskaya

Publikováno v: Nature Communications, Vol 13, Iss 1, Pp 1-18 (2022)

Mitochondrial Ca2+ homeostasis is reported to influence cellular senescence. Here the authors show that TRPC3 limits senescence by inhibiting IP3R-mediated Ca2+ release and ER mitochondria Ca2+ transfer and that the downregulation of TRPC3 in stromal

Externí odkaz: https://doaj.org/article/18e1a197a54f4fbebb56df91fdd44151

Transmembrane BAX Inhibitor-1 Motif Containing Protein 5 (TMBIM5) Sustains Mitochondrial Structure, Shape, and Function by Impacting the Mitochondrial Protein Synthesis Machinery

Autor: Bruno Seitaj, Felicia Maull, Li Zhang, Verena Wüllner, Christina Wolf, Philipp Schippers, Rita La Rovere, Ute Distler, Stefan Tenzer, Jan B. Parys, Geert Bultynck, Axel Methner

Publikováno v: Cells, Vol 9, Iss 10, p 2147 (2020)

The Transmembrane Bax Inhibitor-1 motif (TMBIM)-containing protein family is evolutionarily conserved and has been implicated in cell death susceptibility. The only member with a mitochondrial localization is TMBIM5 (also known as GHITM or MICS1), wh

Externí odkaz: https://doaj.org/article/83025d6a4797438f829a65f8d382a769

IP3 Receptor-Mediated Calcium Signaling and Its Role in Autophagy in Cancer

Autor: Elzbieta Kania, Gemma Roest, Tim Vervliet, Jan B. Parys, Geert Bultynck

Publikováno v: Frontiers in Oncology, Vol 7 (2017)

Calcium ions (Ca2+) play a complex role in orchestrating diverse cellular processes, including cell death and survival. To trigger signaling cascades, intracellular Ca2+ is shuffled between the cytoplasm and the major Ca2+ stores, the endoplasmic ret

Externí odkaz: https://doaj.org/article/b3cbeb67757e4bff8c51a1ce0279eb94

TMBIM5 loss of function alters mitochondrial matrix ion homeostasis and causes a skeletal myopathy

Autor: Li Zhang, Felicia Dietsche, Bruno Seitaj, Liliana Rojas-Charry, Nadina Latchman, Dhanendra Tomar, Rob CI Wüst, Alexander Nickel, Katrin BM Frauenknecht, Benedikt Schoser, Sven Schumann, Michael J Schmeisser, Johannes vom Berg, Thorsten Buch, Stefanie Finger, Philip Wenzel, Christoph Maack, John W Elrod, Jan B Parys, Geert Bultynck, Axel Methner

Publikováno v: Life science alliance, 5(10):e202201478, 1-15. Rockefeller University Press
Zhang, L, Dietsche, F, Seitaj, B, Rojas-Charry, L, Latchman, N, Tomar, D, Wüst, R C, Nickel, A, Frauenknecht, K B, Schoser, B, Schumann, S, Schmeisser, M J, Vom Berg, J, Buch, T, Finger, S, Wenzel, P, Maack, C, Elrod, J W, Parys, J B, Bultynck, G & Methner, A 2022, ' TMBIM5 loss of function alters mitochondrial matrix ion homeostasis and causes a skeletal myopathy ', Life science alliance, vol. 5, no. 10, e202201478, pp. 1-15 . https://doi.org/10.26508/lsa.202201478

Ion fluxes across the inner mitochondrial membrane control mitochondrial volume, energy production, and apoptosis. TMBIM5, a highly conserved protein with homology to putative pH-dependent ion channels, is involved in the maintenance of mitochondrial

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9c011d27b2946bcb5b6358afd11e5522
https://pubmed.ncbi.nlm.nih.gov/35715207