A single motif responsible for ubiquitin recognition and monoubiquitination in endocytic proteins View Full Text


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Article Info

DATE

2002-03

AUTHORS

Simona Polo, Sara Sigismund, Mario Faretta, Monica Guidi, Maria Rosaria Capua, Giovanna Bossi, Hong Chen, Pietro De Camilli, Pier Paolo Di Fiore

ABSTRACT

Ubiquitination is a post-translation modification in which ubiquitin chains or single ubiquitin molecules are appended to target proteins, giving rise to poly- or monoubiquitination, respectively1,2,3,4. Polyubiquitination targets proteins for destruction by the proteasome. The role of monoubiquitination is less understood, although a function in membrane trafficking is emerging, at least in yeast1,3,5. Here we report that a short amino-acid stretch at the carboxy-termini of the monoubiquitinated endocytic proteins Eps15 and eps15R is indispensable for their monoubiquitination. A similar sequence, also required for this modification, is found in other cytosolic endocytic proteins, such as epsins and Hrs. These sequences comprise a protein motif, UIM (ref. 6), which has been proposed to bind to ubiquitin. We confirm this for the UIMs of eps15, eps15R, epsins and Hrs. Thus, the same motif in several endocytic proteins is responsible for ubiquitin recognition and monoubiquitination. Our results predict the existence of a UIM:ubiquitin-based intracellular network. Eps15/eps15R, epsins and Hrs may function as adaptors between ubiquitinated membrane cargo and either the clathrin coat or other endocytic scaffolds. In addition, through their own ubiquitination, they may further contribute to the amplification of this network in the endocytic pathway. More... »

PAGES

451-455

References to SciGraph publications

  • 1998-07. A functional PtdIns(3)P-binding motif in NATURE
  • 2001-03. Protein regulation by monoubiquitin in NATURE REVIEWS MOLECULAR CELL BIOLOGY
  • 1998-07. FYVE fingers bind PtdIns(3)P in NATURE
  • 1998-08. Epsin is an EH-domain-binding protein implicated in clathrin-mediated endocytosis in NATURE
  • 2001-03. Themes and variations on ubiquitylation in NATURE REVIEWS MOLECULAR CELL BIOLOGY
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    http://scigraph.springernature.com/pub.10.1038/416451a

    DOI

    http://dx.doi.org/10.1038/416451a

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1017281203

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/11919637


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