Mechanism of adrenergic CaV1.2 stimulation revealed by proximity proteomics

The PRIDE database and related tools and resources in 2019: improving support for quantification data

Pérez-Riverol, Y., Csordas, A., Bai, J.-W., Bernal-Llinares, M., Hewapathirana, S., Kundu, D. J., Inuganti, A., Griss, J., Mayer, G., Eisenacher, M., et al. (2018) · Nucleic Acids Res. · doi:10.1093/nar/gky1106 · Cited by 6,216

BiNGO: a Cytoscape plugin to assess overrepresentation of Gene Ontology categories in Biological Networks

Maere, S., Heymans, K., & Kuiper, M. T. R. (2005) · Computer applications in the biosciences · doi:10.1093/bioinformatics/bti551 · Cited by 4,163

Sequence and structure-based prediction of eukaryotic protein phosphorylation sites

Blom, N., Gammeltoft, S., & Brunak, S. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.3310 · Cited by 3,212

PKA Phosphorylation Dissociates FKBP12.6 from the Calcium Release Channel (Ryanodine Receptor)

Marx, S. O., Reiken, S. R., Hisamatsu, Y., Jayaraman, T., Burkhoff, D., Rosemblit, N., & Marks, A. R. (2000) · Cell · doi:10.1016/s0092-8674(00)80847-8 · Cited by 1,981

A tissue-specific atlas of mouse protein phosphorylation and expression

Huttlin, E. L., Jedrychowski, M. P., Elias, J. E., Goswami, T., Rad, R., Beausoleil, S. A., Villén, J., Haas, W., Sowa, M. E., & Gygi, S. P. (2010) · Cell · doi:10.1016/j.cell.2010.12.001 · Cited by 1,778

Scansite 2.0: proteome-wide prediction of cell signaling interactions using short sequence motifs

Obenauer, J. C. (2003) · Nucleic Acids Research · doi:10.1093/nar/gkg584 · Cited by 1,609

A probability-based approach for high-throughput protein phosphorylation analysis and site localization

Beausoleil, S. A., Villén, J., Gerber, S. A., Rush, J., & Gygi, S. P. (2006) · Nature Biotechnology · doi:10.1038/nbt1240 · Cited by 1,577

The importance of intrinsic disorder for protein phosphorylation

Iakoucheva, L. M. (2004) · Nucleic Acids Research · doi:10.1093/nar/gkh253 · Cited by 1,429

Directed evolution of APEX2 for electron microscopy and proximity labeling

Lam, S. S., Martell, J. D., Kamer, K. J., Deerinck, T. J., Ellisman, M. H., Mootha, V. K., & Ting, A. Y. (2014) · Nature Methods · doi:10.1038/nmeth.3179 · Cited by 1,395

Proteomic Mapping of Mitochondria in Living Cells via Spatially Restricted Enzymatic Tagging

Martell, J. D., Ting, A. Y., Rhee, H., Zou, P., Udeshi, N. D., Mootha, V. K., & Carr, S. A. (2012) · DSpace@MIT (Massachusetts Institute of Technology) · Cited by 1,330

Contrôle β-adrénergique du courant calcique de type L cardiaque

Leroy, J., & Fischmeister, R. (2020) · médecine/sciences · doi:10.1051/medsci/2020104 · Cited by 1

Voltage-Dependent Ca2+ Channels

Hofmann, F. B. (2021) · Springer eBooks · doi:10.1007/978-3-030-57401-7_33 · Cited by 1

Membrane Proteins | L-Type Calcium Channels in Health and Disease: The Case of Heart Failure

Katat, A. A., Segura, É., & Parent, L. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-819460-7.00077-3 · Cited by 1

Mapping molecular determinants of Ca V 2.2 inhibition by RGK proteins and homologs in Xenopus oocytesPreprint

Sasson, Y., Subramaniam, S., Buki, T., Almagor, L., Chomsky-Hecht, O., Katz, M., Puhl, H. L., Ikeda, S. R., Dascal, N., & Hirsch, J. A. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.06.21.496996 · Cited by 1

Cardiac gene therapy with PDE2A limits remodeling and arrhythmias in mouse models of heart failure induced by catecholaminesPreprint

Kamel, R., Bourcier, A., Margaria, J. P., Varin, A., Hivonnait, A., Mercier‐Nomé, F., Mika, D., Ghigo, A., Charpentier, F., Algalarrondo, V., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.04.17.537274 · Cited by 1

Paradoxical SERCA dysregulation contributes to atrial fibrillation in a model of diet-induced obesityPreprint

Ponce‐Balbuena, D., Tyrrell, D. J., Cruz‐Cortés, C., Guerrero‐Serna, G., da Rocha, A. M., Herron, T. J., Song, J., Raza, D. S., ANUMONWO, J. M. B., Goldstein, D. R., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.08.02.606385 · Cited by 1

Probing the Ca V 1.2 interactome in heart failure identifies a positive modulator of inotropy and lusitropyPreprint

Rodriques, A., Liu, G., Katchman, A. N., Zakharov, S. I., Wan, E. Y., Kalocsay, M., Eisert, R. J., Bradshaw, G. A., Chen, B.-X., Yang, L., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.05.08.652977 · Cited by 2

A Unifying Mechanism for Synaptic Amyloid β Toxicity β Adrenergic Potentiation of the Ca 2+ Channel CaV1.2 by Amyloid βPreprint

Bartels, P. H., Rougé, S. L. S., Scripter, J. D., Zeng, Z., Estrada‐Tobar, Z. M., Price, J., Jacobi, A. A., Berumen, R. A., Ho, S., Avedisyan, A., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.04.25.720803 · Cited by 1

Rad Modulation of the L-type Calcium Channel Confers Systolic Advantage in the Heart

Ahern, B. M. (2021) · UKnowledge (University of Kentucky) · doi:10.13023/etd.2021.146

In aging hearts β-adrenergic stimulation can lead to a decrease, instead of an increase, in the slow delayed rectifier current: A new risk factor for aging-related arrhythmia?

Tseng, G. (2021) · Heart Rhythm · doi:10.1016/j.hrthm.2021.09.020

ER-PM contacts and CRAC signaling in muscle cells

Sun, A., YiLan, C. H. E. N., Ji, J., & Wang, Y. (2021) · Scientia Sinica Vitae · doi:10.1360/ssv-2021-0143

Mapping of the autophagosomal degradome identifies IL-7Rα as key cargo in proliferating CD4+ T-cellsPreprint

Zhou, D., Borsa, M., Puleston, D. J., Zellner, S., Capera, J., Sanderson, S., Jostins, L., Behrends, C., Alsaleh, G., & Simon, A. K. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.12.08.471825

Voltage-Dependent Ca2+ Channels

Hofmann, F. B. (2021) · Springer eBooks · doi:10.1007/978-3-030-21573-6_33-1

Vasculature remodeling by pressure, caveolae, calcium, and kinases

Marx, A. M., & Marx, S. O. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2204968119

Adrenergic augmentation of cardiac contractility requires Rad phosphorylation

(2022) · Nature Cardiovascular Research · doi:10.1038/s44161-022-00168-9

The Skeletal Muscle Calcium Channel

Flucher, B. E., & Beam, K. G. (2022) · Springer eBooks · doi:10.1007/978-3-031-08881-0_16

A Lived History of Early Calcium Channel Discoveries Over the Past Half-Century

Carbone, E. (2022) · Springer eBooks · doi:10.1007/978-3-031-08881-0_1

Na + /K + ATPase-Ca v 1.2 nanodomain differentially regulates intracellular [Na + ], [Ca 2+ ] and local adrenergic signaling in cardiac myocytesPreprint

Karbowski, M., Boyman, L., Garber, L., Joca, H. C., Verhoeven, N. A., Coleman, A. K., Ward, C. W., Lederer, W. J., & Greiser, M. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.08.31.553598

Tripartite interactions of PKA catalytic subunit and C-terminal domains of cardiac Ca 2+ channel modulate its β-adrenergic regulationPreprint

Oz, S., Sharon, T., Subramaniam, S., Pallien, T., Katz, M., Tsemakhovich, V., Tripathy, D. R., Sasson, G., Chomsky-Hecht, O., Vysochek, L., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.11.28.564875

In vivo proximity proteomics uncovers palmdelphin (PALMD) as a Z-line-associated mitigator of isoproterenol-induced cardiac injuryPreprint

Guo, C., Jardin, B. D., Lin, J., Ambroise, R. L., Wang, Z., Yang, L., Mazumdar, N., Lu, F., Ma, Q., Cao, Y., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.12.06.570334

The good company of T-type calcium channels

Lory, P. (2024) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-023-02903-y

Physiological and pathological roles of protein kinase a in the heart

Zalfo, K. A., & Ali, A. F. (2024) · International Journal of Clinical Biology and Biochemistry · doi:10.33545/26646188.2024.v6.i1b.65

Physiologie de la contraction et de la relaxation cardiaques

Mercadier, J.-J., & Gomez, A. M. (2026) · EMC - Cardiologie · doi:10.1016/s1166-4568(25)49480-7

Neurogranin Unlocks the L-type Ca²⁺ Channel and Directs Calmodulin DeliveryPreprint

Yu, Z., Geng, J., Qiu, S., Zhang, W., He, M., & Liu, X. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.06.20.660829

Casein Kinase 2 Regulates the Intrinsic Activity of L-Type Calcium Currents in Cardiomyocytes

Zhao, J., Broszczak, M., & Parent, L. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26136010

Phosphodiesterase type 1 regulates adenosine 2A receptor-associated cAMP signaling at the plasma membrane to increase myocardial contractilityPreprint

Fitch, M. L., Goncalves, M. A. M., Tang, M. H. Y., Kelly, E. D., Cheung, E. C., Kandula, P., Jones, E., Sornat, S., Sun, O., Zaccolo, M., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.10.03.680406

A RADical approach to treating heart failure

Obeidat, M., & Eisner, D. A. (2025) · Cardiovascular Research · doi:10.1093/cvr/cvaf184

Additional file 1 of Decreased expression of GEM in osteoarthritis cartilage regulates chondrogenic differentiation via Wnt/β-catenin signaling

Gan, L., Deng, Z., Wei, Y., Li, H., & Zhao, L. (2024) · Figshare · doi:10.6084/m9.figshare.26622607

Molecular Symphony of Sympathetic Acceleration: Reframing the Pacemaker Paradigm

Xiao, L., Cai, W., & Valdivia, H. H. (2026) · Circulation Research · doi:10.1161/circresaha.125.327778

L-type channel voltage-dependent facilitation results from asymmetric π-H and π-π quadrangle interactions at DI–DII domainsPreprint

Hoque, A., Khade, V. T., Gopal, E. V., Kate, A. S., Zamponi, G. W., & Sahu, G. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.01.23.701029

Molecular Partners of Voltage-Gated Calcium Channel β and α2δ Auxiliary Subunits: Roles in Channel Complex Regulation and Beyond

Corzo-López, A., Leyva-Leyva, M., González‐Ramírez, R., Sandoval, A., & Felix, R. (2026) · The Journal of Membrane Biology · doi:10.1007/s00232-026-00371-w

ESCRT-Mediated Machinery Directly Drives Cardiac T-tubule Formation

Wang, X., Han, S., Zhang, G., Huang, X., Xu, C., Zhang, J., Zheng, Y., Zhao, P., Lin, T., Feng, Z., et al. (2026) · Circulation Research · doi:10.1161/circresaha.125.327453

Multiscale anisotropic scaffolds enable a biomimetic electro-mechanical myocardial platform for drug discovery and heart repair

Zou, J., Zhang, J., Zhao, Q., Luo, G., Zhang, X., Chen, S., Li, Y., He, Y., Wang, L., & Qiu, X. (2026) · Biomaterials Science · doi:10.1039/d6bm00103c

Progrès dans la compréhension de la régulation adrénergique du couplage excitation-contraction cardiaque et des récepteurs de la ryanodine RyR₂ par la PKA de type I et FKBP12.6

Gandon-Renard, M. (2021) · doi:10.70675/4ccbb154zb1d4z42b8za0dczb89fbc06f7c4

Rôle des canaux calciques de type l cav1.3 et des canaux potassiques activés par les protéines g ikach dans la régulation cholinergique de l'automatisme cardiaque

Talssi, L. (2021) · doi:10.70675/1421053az7cd3z4879z92a6z1485a5df4cc2

Ιmplicatiοn des prοtéines EΡAC dans la régulatiοn de l'activité électrique des cardiοmyοcytes

Boilève, A. (2024) · doi:10.70675/51541e6ez414cz4382zbd80z3a443c12687f

MicroRNA‐210‐mediated mitochondrial reactive oxygen species contribute to Ca V 1.2 channel hyperactivity in uterine arteries of pregnant sheep acclimatized to high‐altitude hypoxia

Hu, X., Song, R., Dasgupta, C., Liu, T., Zhang, M., Mata‐Greenwood, E., Goulopoulou, S., Blood, A. B., & Zhang, L. (2026) · The Journal of Physiology · doi:10.1113/jp290989

An RYR2-interacting fragment of MYBPC3 mitigates arrhythmia in human iPSC-CM and mouse models of CPVT

Lu, F., Wu, Z., Chi, S., Li, J., Ponek, A., Liou, C., Ma, Q., Bonde, D., Pavlaki, N., Sweat, M., et al. (2026) · Molecular Therapy · doi:10.1016/j.ymthe.2026.04.030

Industrial settleable particulate matter promote metal(loid) bioaccumulation, metallic nanoparticle internalization and cardiac dysfunction in bullfrog tadpole

Monteiro, D. A., da Costa, R. L., Souza, I. D. C., da Silva, B. H., Fernandes, S. L. A., Carvalho, C. D. S., Monferrán, M. V., Wunderlin, D. A., & Fernandes, M. N. (2026) · Environmental Toxicology and Pharmacology · doi:10.1016/j.etap.2026.105079

Application of Proximity-Labeling Techniques in Plants: A Review of Successful Cases

Yang, Z., Yang, S., & Meng, Q. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27167227

A Seven Amino Acid Long Region in the Cardiac Cav1.2, Encompassing Ser1487, Is Essential for Mice Embryonic Development and “Fight or Flight” Responses

Jenkins, C., Szappanos, H. C., Dyrda, A., Er, T., Petegem, F. V., & Hool, L. C. (2026) · Cells · doi:10.3390/cells15181655

Dual Role of CACNA1C/CaV1.2 in Cardiac and Neuropsychiatric Disease

Königstein, D., Kisko, T. M., Michels, S., Alferink, J., Wöhr, M., Culmsee, C., & Kockskämper, J. (2026) · Biomolecules · doi:10.3390/biom16101459

Proximity labeling technologies for multiscale spatial proteomics: from organelle contact sites to intercellular and inter-organ communication

Chen, D., Zhao, H., Zhao, H., & Wang, J. (2026) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2026.154761

Reconstitution of β-adrenergic regulation of Ca V 1.2: Rad-dependent and Rad-independent protein kinase A mechanisms

Katz, M., Subramaniam, S., Chomsky-Hecht, O., Tsemakhovich, V., Belkacemi, A., Flockerzi, V., Klußmann, E., Hirsch, J. A., Weiss, S., & Dascal, N. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2100021118 · Cited by 27

Adrenergic augmentation of cardiac contractility requires Rad phosphorylation

(2022) · Nature Cardiovascular Research · doi:10.1038/s44161-022-00168-9

Anchored PKA synchronizes adrenergic phosphoregulation of cardiac Cav1.2 channels

Wang, L., Chen, Y., Li, J., Westenbroek, R. E., Philyaw, T., Zheng, N., Scott, J. D., Liu, Q., & Catterall, W. A. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.107656 · Cited by 8

The quest to identify the mechanism underlying adrenergic regulation of cardiac Ca2+ channels

Roybal, D., Hennessey, J. A., & Marx, S. O. (2020) · Channels · doi:10.1080/19336950.2020.1740502 · Cited by 13

Rad regulation of CaV1.2 channels controls cardiac fight-or-flight response

Papa, A. E., Zakharov, S. I., Katchman, A. N., Kushner, J., Chen, B.-X., Yang, L., Liu, G., Jimenez, A. S., Eisert, R. J., Bradshaw, G. A., et al. (2022) · Nature Cardiovascular Research · doi:10.1038/s44161-022-00157-y · Cited by 54