SUMMARY Tail-anchored (TA) proteins are posttranslationally inserted into either the endoplasmic reticulum (ER) or the mitochondrial outer membrane. The C-terminal transmembrane domains (TMDs) of TA proteins enable their many essential cellular functions by specifying the membrane target, but how cells process these targeting signals is poorly understood. Here, we reveal the composition of a conserved multiprotein TMD recognition complex (TRC) and show that distinct TRC subunits recognize the two types of TMD signals. By engineering mutations in a mitochondrial TMD, we switch over its TRC subunit recognition, thus leading to its misinsertion into the ER. Biochemical reconstitution with purified components demonstrates that TRC tethers and enzymatically activates Get3 to selectively hand off ER-bound TA proteins to Get3. Thus, ER-bound TA proteins are sorted at the top of a TMD chaperone cascade that culminates with the formation of Get3-TA protein complexes, which are recruited to the ER membrane for insertion.

Our study shows that some form of Thebesian valve is present in the majority of hearts (>70%). Of these, a significant minority (16%) had a valve morphology (covering >75% of the ostium, a fibrous, fibromuscular, or muscular composition, and devoid of fenestrations) that makes them a 'potentially complicating' structure interfering with the cannulation of the CS.

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The pericardium provides an enclosed lubricated space for the beating heart and functions to fix the heart in the chest cavity relative to adjacent organs. Pericardial pathophysiology is often manifested in a spectrum of distinct cardiac and systemic disease states. The pericardial response to injury typically involves a spectrum of inflammation with both acute and chronic features and/or fluid accumulation. Recent advances in imaging methods have refined the diagnosis and therapy of pericardial disease. This article presents the anatomy and physiology of pericardial disease and the clinical approach for diagnosis and treatment.

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