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Mutations in HSP27 cause Charcot\u2010Marie\u2010Tooth (CMT) disease, the most common inherited disorder of the peripheral nervous system. A particularly severe form of CMT disease is triggered by the P182L mutation in the highly conserved IxI\/V motif of the disordered C\u2010terminal region, which interacts weakly with the structured core domain of HSP27. Here, we observed that the P182L mutation disrupts the chaperone activity and significantly increases the size of HSP27 oligomers formed\n                    <jats:italic>in vivo<\/jats:italic>\n                    , including in motor neurons differentiated from CMT patient\u2010derived stem cells. Using NMR spectroscopy, we determined that the P182L mutation decreases the affinity of the HSP27 IxI\/V motif for its own core domain, leaving this binding site more accessible for other IxI\/V\u2010containing proteins. We identified multiple IxI\/V\u2010bearing proteins that bind with higher affinity to the P182L variant due to the increased availability of the IxI\/V\u2010binding site. Our results provide a mechanistic basis for the impact of the P182L mutation on HSP27 and suggest that the IxI\/V motif plays an important, regulatory role in modulating protein\u2013protein interactions.\n                  <\/jats:p>","DOI":"10.15252\/embj.2019103811","type":"journal-article","created":{"date-parts":[[2021,3,1]],"date-time":"2021-03-01T03:33:06Z","timestamp":1614569586000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":22,"title":["A weakened interface in the P182L variant of HSP27 associated with severe Charcot\u2010Marie\u2010Tooth neuropathy causes aberrant binding to interacting proteins"],"prefix":"10.1038","volume":"40","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-5163-2276","authenticated-orcid":false,"given":"T","family":"Reid Alderson","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9430-917X","authenticated-orcid":false,"given":"Elias","family":"Adriaenssens","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2784-2470","authenticated-orcid":false,"given":"Bob","family":"Asselbergh","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9152-6555","authenticated-orcid":false,"given":"Iva","family":"Priti\u0161anac","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jonas","family":"Van Lent","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Heidi Y","family":"Gastall","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marielle A","family":"W\u00e4lti","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"John M","family":"Louis","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2162-0933","authenticated-orcid":false,"given":"Vincent","family":"Timmerman","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7579-8844","authenticated-orcid":false,"given":"Andrew J","family":"Baldwin","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1507-3742","authenticated-orcid":false,"given":"Justin","family":"LP Benesch","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2021,3,1]]},"reference":[{"key":"BFEMBJ2019103811_CR1","doi-asserted-by":"crossref","first-page":"347","DOI":"10.1093\/hmg\/ddi452","volume":"15","author":"S Ackerley","year":"2006","unstructured":"Ackerley S, James PA, Kalli A, French S, Davies KE, Talbot K (2006) A mutation in the small heat\u2010shock protein HSPB1 leading to distal hereditary motor neuronopathy disrupts neurofilament assembly and the axonal transport of specific cellular cargoes. 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