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Biology subjects

Kavanagh, D. M.

Publications and source records attributed to Kavanagh, D. M..

2 recordsLinked to original sources

Male sex hormone and reduced plakoglobin jointly impair atrial conduction and cardiac sodium currents

Androgenic anabolic steroids (AAS) are commonly abused by young men. Male sex associates with earlier manifestation of common and rare cardiac conditions including atrial fibrillation and arrhythmogenic right ventricular cardiomyopathy (ARVC). Clinical data suggest an atrial involvement in ARVC. The disease is caused by desmosomal gene defects such as reduced plakoglobin expression. Analysis of clinical records from 146 ARVC patients identified male preponderance and increased prevalence of atrial arrhythmias in patients with definite ARVC. Definite patients displayed ECG changes suggesting atrial remodelling. To study mechanisms of atrial remodelling due to desmosomal vulnerability and AAS, young adult male mice, heterozygously deficient for plakoglobin (Plako+/-) and wildtype (WT) littermates, were chronically exposed to 5-dihydrotestosterone (DHT) or placebo. DHT increased atrial expression of pro-hypertrophic, fibrotic and inflammatory transcripts. DHT caused atrial conduction slowing, decreased peak sodium current density, reduced action potential amplitude and lowered the peak depolarisation rate in Plako+/- but not WT atria. Super-resolution microscopy revealed a reduction in Nav1.5 clustering in Plako+/- atrial cardiomyocytes following DHT exposure. These data reveal that AAS combined with plakoglobin deficiency cause pathological atrial electrical remodelling in young male hearts. AAS abuse may increase the risk of atrial myopathy in males with desmosomal gene variants.

molecular biology↗

A novel VPS33A interaction motif is a master-switch controlling the inhibition and promotion of mammalian Stx17 interactions with SNAP29 and VAMP7 during autophagy

Autophagosome clearance is accomplished by SNARE-mediated fusion of the vesicle membrane with the endolysosome. This must be carefully regulated to maintain the organisation of the membrane system and prevent mistargeted degradation. Here, we dissect the autophagosomal SNARE complex pathway and its regulation using FLIM-FRET as a readout of protein interaction in situ. We show that within the spatio-temporal framework of the cell, autophagosomal Stx17 preferentially heterodimerises with SNAP29, subsequently associating with VAMP7, not VAMP8 as currently believed. Additionally, we identify for the first time multi-modal regulation of SNARE assembly by the SM protein VPS33A, finding parallels and differences with other syntaxin-SM interactions and suggesting a unifying model of SM regulation. Contrary to current theory, the Stx17 N-peptide interacts in a positionally conserved, but mechanistically divergent manner with VPS33A, providing a late go, no-go step for autophagic fusion via a phosphoserine master-switch.

cell biology↗