{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Vogel A"],"funding":["Oregon State University","National Institutes of Health","National Science Foundation of Sri Lanka","M.J. Murdock Charitable Trust","NIH HHS"],"pagination":["e4295"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8994507"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["31(5)"],"pubmed_abstract":["Multivalent complexes formed between the cancer-promoting transcriptional co-activator, Yes-associated protein (YAP), and proteins containing short linear motifs of type PPxY modulate cell proliferation and are attractive therapeutic targets. However, challenges producing PPxY polypeptides containing the full binding domain has limited understanding of the assembly process. Here, we successfully produced a polypeptide containing the complete set of three PPxY binding sites of Angiomotin-like 1 (AMOTL1), a scaffolding protein that regulates the nucleo-cytoplasmic shuttling of YAP via WW-PPxY interactions. Using an array of biophysical techniques including isothermal titration calorimetry, size-exclusion chromatography coupled to multi-angle light scattering, and solution nuclear magnetic re"],"journal":["Protein science : a publication of the Protein Society"],"pubmed_title":["Multivalent Angiomotin-like 1 and Yes-associated protein form a dynamic complex."],"pmcid":["PMC8994507"],"funding_grant_id":["S10 OD018518","2014162","MCB‐2114544","1S10OD018518"],"pubmed_authors":["Crawford A","Vogel A","Nyarko A"],"additional_accession":[]},"is_claimable":false,"name":"Multivalent Angiomotin-like 1 and Yes-associated protein form a dynamic complex.","description":"Multivalent complexes formed between the cancer-promoting transcriptional co-activator, Yes-associated protein (YAP), and proteins containing short linear motifs of type PPxY modulate cell proliferation and are attractive therapeutic targets. However, challenges producing PPxY polypeptides containing the full binding domain has limited understanding of the assembly process. Here, we successfully produced a polypeptide containing the complete set of three PPxY binding sites of Angiomotin-like 1 (AMOTL1), a scaffolding protein that regulates the nucleo-cytoplasmic shuttling of YAP via WW-PPxY interactions. Using an array of biophysical techniques including isothermal titration calorimetry, size-exclusion chromatography coupled to multi-angle light scattering, and solution nuclear magnetic re","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 May","modification":"2026-07-14T20:21:59.001Z","creation":"2024-11-07T10:32:22.469Z"},"accession":"S-EPMC8994507","cross_references":{"pubmed":["35481651"],"doi":["10.1002/pro.4295"]}}