The functional versatility of metacaspase proteases has been established by reports of their involvement in non-apoptotic cellular processes, in addition to their canonical role in apoptosis/programmed cell death. While the budding yeast metacaspase Yca1 has been well characterized for its role in cell death regulation, more recent examinations suggest that the protease may be involved in key processes that increase survival and fitness. More specifically, examinations suggest that Yca1 is central to maintaining cellular proteostasis as it interacts with major components involved in protein biosynthesis and functions to limit aggregate deposition. Here, we describe the methods utilized to analyze the role Yca1 in proteostasis.
This is a preview of subscription content, log in to check access.
Springer Nature is developing a new tool to find and evaluate Protocols. Learn more
Aravind L, Koonin EV (2002) Classification of the caspase–hemoglobinase fold: detection of new families and implications for the origin of the eukaryotic separins. Proteins 46:355–367PubMedCrossRefGoogle Scholar
Uren AG, O’Rourke K, Aravind L et al (2000) Identification of paracaspases and metacaspases: two ancient families of caspase-like proteins one of which plays a key role in MALT lymphoma. Mol Cell 6:961–967PubMedGoogle Scholar
Mitchell L, Lambert JP, Gerdes M et al (2008) Functional dissection of the NuA4 histone acetyltransferase reveals its role as a genetic hub and that Eaf1 is essential for complex integrity. Mol Cell Biol 28:2244–2256PubMedCentralPubMedCrossRefGoogle Scholar
Shrestha A, Brunette S, Puente LG et al (2013) The role of Yca1 in proteostasis. Yca1 regulates the composition of the insoluble proteome. J Proteomics 81:24–30PubMedCrossRefGoogle Scholar
Parsell DA, Kowal AS, Singer MA et al (1994) Protein disaggregation mediated by heat-shock protein Hsp104. Nature 372:475–478PubMedCrossRefGoogle Scholar
Glover JR, Lindquist S (1998) Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins. Cell 94:73–82PubMedCrossRefGoogle Scholar
Cashikar AG, Duendald M, Lindquist SL (2005) A chaperone pathway in protein disaggregation. Hsp26 alters the nature of protein aggregates to facilitate reactivation by Hsp104. J Biol Chem 280:23869–23875PubMedCentralPubMedCrossRefGoogle Scholar
Haslbeck M, Miess A, Stromer T et al (2005) Disassembling protein aggregates in the yeast cytosol. The cooperation of Hsp26 with Ssa1 and Hsp104. J Biol Chem 280:23861–23868PubMedCrossRefGoogle Scholar