ArticleMolecular and cellular biology2003
YPXL/I is a protein interaction motif recognized by aspergillus PalA and its human homologue, AIP1/Alix.
Article in Molecular and cellular biology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 77 papers.
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77 citing papers in PubMed, 156 citations in OpenAlex.
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- The HIV-1 late domain-2 S40A polymorphism in antiretroviral (or ART)-exposed individuals influences protease inhibitor susceptibility.Retrovirology · 2016Article
- Mutational analysis of the Aspergillus ambient pH receptor PalH underscores its potential as a target for antifungal compounds.Molecular microbiology · 2016Article
- Ammonia activates pacC and patulin accumulation in an acidic environment during apple colonization by Penicillium expansum.Molecular plant pathology · 2016Article
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17 more citing papers are in PubMed but not listed here.
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5 authors at 2 institutions in 2 countries.
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No grant is acknowledged in the PubMed record.
Abstract
The zinc finger transcription factor PacC undergoes two-step proteolytic activation in response to alkaline ambient pH. PalA is a component of the fungal ambient pH signal transduction pathway. Its mammalian homologue AIP1/Alix interacts with the apoptosis-linked protein ALG-2. We show that both PalA and AIP1/Alix recognize a protein-protein binding motif that we denote YPXL/I, where Tyr, Pro, and Leu/Ile are crucial for its interactive properties. Two such motifs flanking the signaling protease cleavage site mediate direct binding of PalA to PacC, required for the first and only pH-regulated cleavage of this transcription factor. PalA can bind the "closed" (i.e., wild-type full-length) conformer of PacC, suggesting that PalA binding constitutes the first stage in the two-step proteolytic cascade, recruiting or facilitating access of the signaling protease, presumably PalB. In addition to recognizing YPXL/I motifs, both PalA and AIP1/Alix interact with the Aspergillus class E Vps protein Vps32 homologue, a member of a protein complex involved in the early steps of the multivesicular body pathway, suggesting that this interaction is an additional feature of proteins of the PalA/AIP1/Alix family.
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