Influence of protein-micelle ratios and cysteine residues on the kinetic stability and unfolding rates of human mitochondrial VDAC-2.

Autor: Svetlana Rajkumar Maurya, Radhakrishnan Mahalakshmi

Publikováno v: PLoS ONE, Vol 9, Iss 1, p e87701 (2014)

Delineating the kinetic and thermodynamic factors which contribute to the stability of transmembrane β-barrels is critical to gain an in-depth understanding of membrane protein behavior. Human mitochondrial voltage-dependent anion channel isoform 2

Externí odkaz: https://doaj.org/article/1d14d7e65ead4d4e833109a8d7eba630

Disruption of Ca 2+ i Homeostasis and Connexin 43 Hemichannel Function in the Right Ventricle Precedes Overt Arrhythmogenic Cardiomyopathy in Plakophilin-2–Deficient Mice

Autor: Marta Pérez-Hernández, Jérôme Montnach, Sun-Hee Woo, Svetlana Rajkumar Maurya, Mingliang Zhang, Alicia Lundby, Xianming Lin, Carolina Vasquez, Yandong Yin, Francisco J. Alvarado, Eli Rothenberg, Feng-Xia Liang, Adriana Heguy, Marina Cerrone, Joon-Chul Kim, Gregory E. Morley, Héctor H. Valdivia, Mario Delmar

Publikováno v: Kim, J-C, Perez-Hernandez, M, Alvarado, F J, Maurya, S R, Montnach, J, Yin, Y, Zhang, M, Lin, X, Vasquez, C, Heguy, A, Liang, F-X, Woo, S-H, Morley, G E, Rothenberg, E, Lundby, A, Valdivia, H H, Cerrone, M & Delmar, M 2019, ' Disruption of Ca 2+ i Homeostasis and Connexin 43 Hemichannel Function in the Right Ventricle Precedes Overt Arrhythmogenic Cardiomyopathy in Plakophilin-2-Deficient Mice ', Circulation, vol. 140, no. 12, pp. 1015-1030 . https://doi.org/10.1161/CIRCULATIONAHA.119.039710

Background: Plakophilin-2 (PKP2) is classically defined as a desmosomal protein. Mutations in PKP2 associate with most cases of gene-positive arrhythmogenic right ventricular cardiomyopathy. A better understanding of PKP2 cardiac biology can help elu

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::34dea25673075913d89571ac28156e0f
https://doi.org/10.1161/circulationaha.119.039710

Oncogenic Mutations Rewire Signaling Pathways by Switching Protein Recruitment to Phosphotyrosine Sites

Autor: Marie Kveiborg, Blanca Lopez Mendez, Kristina B. Emdal, Chiara Francavilla, Jan C. Refsgaard, Jesper V. Olsen, Svetlana Rajkumar Maurya, Anna Secher, Giulia Franciosa, Alicia Lundby, Lars Juhl Jensen, Indranil Paul, Sebastian Gnosa, Christian D. Kelstrup, Dorte B. Bekker-Jensen, Guillermo Montoya

Publikováno v: Lundby, A, Franciosa, G, Emdal, K B, Refsgaard, J C, Gnosa, S P, Bekker-Jensen, D B, Secher, A, Maurya, S R, Paul, I, Mendez, B L, Kelstrup, C D, Francavilla, C, Kveiborg, M, Montoya, G, Jensen, L J & Olsen, J V 2019, ' Oncogenic Mutations Rewire Signaling Pathways by Switching Protein Recruitment to Phosphotyrosine Sites ', Cell, vol. 179, no. 2, pp. 543-560 . https://doi.org/10.1016/j.cell.2019.09.008
Lundby, A, Franciosa, G, Emdal, K B, Refsgaard, J C, Gnosa, S P, Bekker-jensen, D B, Secher, A, Maurya, S R, Paul, I, Mendez, B L, Kelstrup, C D, Francavilla, C, Kveiborg, M, Montoya, G, Jensen, L J & Olsen, J V 2019, ' Oncogenic Mutations Rewire Signaling Pathways by Switching Protein Recruitment to Phosphotyrosine Sites ', Cell, vol. 179, no. 2, pp. 543-560.e26 . https://doi.org/10.1016/j.cell.2019.09.008
Cell

Tyrosine phosphorylation regulates multi-layered signaling networks with broad implications in (patho)physiology, but high-throughput methods for functional annotation of phosphotyrosine sites are lacking. To decipher phosphotyrosine signaling direct

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5df6d528dfc94a7a5714f79ce8e5fb20
https://pubmed.ncbi.nlm.nih.gov/31585087

Mitochondrial VDAC2 and cell homeostasis: highlighting hidden structural features and unique functionalities

Autor: Radhakrishnan Mahalakshmi, Svetlana Rajkumar Maurya

Publikováno v: Biological Reviews. 92:1843-1858

Voltage-dependent anion channels (VDACs) are the gateway to mitochondrial processes, interlinking the cytosolic and mitochondrial compartments. The mitochondrion acts as a storehouse for cytochrome c, the effector of apoptosis, and hence VDACs become

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::a1d75996e1eb54a56474bd1e50213d0f
https://doi.org/10.1111/brv.12311

N-helix and Cysteines Inter-regulate Human Mitochondrial VDAC-2 Function and Biochemistry

Autor: Svetlana Rajkumar Maurya, Radhakrishnan Mahalakshmi

Publikováno v: The Journal of Biological Chemistry

Human voltage-dependent anion channel-2 (hVDAC-2) functions primarily as the crucial anti-apoptotic protein in the outer mitochondrial membrane, and additionally as a gated bidirectional metabolite transporter. The N-terminal helix (NTH), involved in

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1708dfce03efac9647679c7b04e9eddb
https://doi.org/10.1074/jbc.m115.693978