The Structural and Biochemical Characterization of Members of the Mammalian TA Protein Sorting Complex

Abstract

Tail-anchored (TA) proteins are ubiquitous in eukaryotes and fulfill various important functions in the cell, such as the mediation of cell-cell contact and apoptosis signaling. Because they are anchored to the membrane by a short transmembrane domain (TMD) at the C-terminus, they cannot utilize the cotranslational signal recognition particle (SRP) pathway. Recent biochemical and structural studies have helped us identify and elucidate the details of the TA protein targeting pathway in yeast, also known as the Guided Entry of TA protein (GET) pathway. A homologous pathway, the TMD Recognition Complex (TRC) pathway, has been identified but details of this pathway remain elusive. In this study, we have structurally and biochemically characterized Bag6 and Ubl4Apreviously shown to be crucial in the recognition and delivery TA proteins from the ribosome to TRC40.

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