{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,2]],"date-time":"2026-10-02T23:19:07Z","timestamp":1790983147347,"version":"4.1.0"},"reference-count":47,"publisher":"American Society for Cell Biology (ASCB)","issue":"7","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["MBoC"],"published-print":{"date-parts":[[2004,7]]},"abstract":"<jats:p> Targeting of peroxisomal membrane proteins (PMPs) is a multistep process that requires not only recognition of PMPs in the cytosol but also their insertion into the peroxisomal membrane. As a consequence, targeting signals of PMPs (mPTS) are rather complex. A candidate protein for the PMP recognition event is Pex19p, which interacts with most PMPs. However, the respective Pex19p-binding sites are ill-defined and it is currently disputed whether these sites are contained within mPTS. By using synthetic peptide scans and yeast two-hybrid analyses, we determined and characterized Pex19p-binding sites in Pex11p and Pex13p, two PMPs from Saccharomyces cerevisiae. The sites turned out to be composed of a short helical motif with a minimal length of 11 amino acids. With the acquired data, it proved possible to predict and experimentally verify Pex19p-binding sites in several other PMPs by applying a pattern search and a prediction matrix. A peroxisomally targeted Pex13p fragment became mislocalized to the endoplasmic reticulum in the absence of its Pex19p-binding site. By adding the heterologous binding site of Pex11p, peroxisomal targeting of the Pex13p fragment was restored. We conclude that Pex19p-binding sites are well-defined entities that represent an essential part of the mPTS. <\/jats:p>","DOI":"10.1091\/mbc.e04-03-0188","type":"journal-article","created":{"date-parts":[[2004,5,11]],"date-time":"2004-05-11T00:54:37Z","timestamp":1084236877000},"page":"3406-3417","source":"Crossref","is-referenced-by-count":155,"title":["Peroxisomal Membrane Proteins Contain Common Pex19p-binding Sites that Are an Integral Part of Their Targeting Signals"],"prefix":"10.1091","volume":"15","author":[{"given":"Hanspeter","family":"Rottensteiner","sequence":"first","affiliation":[{"name":"Institut f\u00fcr Physiologische Chemie, Ruhr-Universit\u00e4t Bochum, 44780 Bochum, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Achim","family":"Kramer","sequence":"additional","affiliation":[{"name":"Institut f\u00fcr Medizinische Immunologie, Universit\u00e4tsklinikum Charit\u00e9, 10115 Berlin, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Stephan","family":"Lorenzen","sequence":"additional","affiliation":[{"name":"Institut f\u00fcr Biochemie, Universit\u00e4tsklinikum Charit\u00e9, 10115 Berlin, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Katharina","family":"Stein","sequence":"additional","affiliation":[{"name":"Institut f\u00fcr Physiologische Chemie, Ruhr-Universit\u00e4t Bochum, 44780 Bochum, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christiane","family":"Landgraf","sequence":"additional","affiliation":[{"name":"Institut f\u00fcr Medizinische Immunologie, Universit\u00e4tsklinikum Charit\u00e9, 10115 Berlin, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rudolf","family":"Volkmer-Engert","sequence":"additional","affiliation":[{"name":"Institut f\u00fcr Medizinische Immunologie, Universit\u00e4tsklinikum Charit\u00e9, 10115 Berlin, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ralf","family":"Erdmann","sequence":"additional","affiliation":[{"name":"Institut f\u00fcr Physiologische Chemie, Ruhr-Universit\u00e4t Bochum, 44780 Bochum, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1076","reference":[{"key":"atypb1","doi-asserted-by":"crossref","unstructured":"Albertini, M., Rehling, P., Erdmann, R., Girzalsky, W., Kiel, J.A., Veenhuis, M., and Kunau, W.H. 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