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MINDY-1 Is a Member of an Evolutionarily Conserved and Structurally Distinct New Family of Deubiquitinating Enzymes
Open accessAbstract
Deubiquitinating enzymes (DUBs) remove ubiquitin (Ub) from Ub-conjugated substrates to regulate the functional outcome of ubiquitylation. Here we report the discovery of a new family of DUBs, which we have named MINDY (motif interacting with Ub-containing novel DUB family). Found in all eukaryotes, MINDY-family DUBs are highly selective at cleaving K48-linked polyUb, a signal that targets proteins for degradation. We identify the catalytic activity to be encoded within a previously unannotated domain, the crystal structure of which reveals a distinct protein fold with no homology to any of the known DUBs. The crystal structure of MINDY-1 (also known as FAM63A) in complex with propargylated Ub reveals conformational changes that realign the active site for catalysis. MINDY-1 prefers cleaving long polyUb chains and works by trimming chains from the distal end. Collectively, our results reveal a new family of DUBs that may have specialized roles in regulating proteostasis.
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Self-citation
Metadata
- Authors
- Abdul Rehman, S. A., Kristariyanto, Y. A., Choi, S.-Y., Nkosi, P. J., Weidlich, S., Labib, K., Hofmann, K., & Kulathu, Y.
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2016-07
- Volume
- 63
- Issue
- 1
- Pages
- 146-155
- ISSN
- 1097-2765 (ISSN-L)
- OpenAlex
- W2409179396
- Cited by
- 363
- References
- 40
- FWCI
- 15.95
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Abdul Rehman, S. A., Kristariyanto, Y. A., Choi, S.-Y., Nkosi, P. J., Weidlich, S., Labib, K., Hofmann, K., & Kulathu, Y. (2016). MINDY-1 Is a Member of an Evolutionarily Conserved and Structurally Distinct New Family of Deubiquitinating Enzymes. Molecular Cell. https://doi.org/10.1016/j.molcel.2016.05.009
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