Author
Listed:
- Simona Polo
(European Institute of Oncology)
- Sara Sigismund
(European Institute of Oncology)
- Mario Faretta
(European Institute of Oncology)
- Monica Guidi
(European Institute of Oncology)
- Maria Rosaria Capua
(European Institute of Oncology)
- Giovanna Bossi
(European Institute of Oncology)
- Hong Chen
(Yale University School of Medicine)
- Pietro De Camilli
(Yale University School of Medicine)
- Pier Paolo Di Fiore
(European Institute of Oncology
IFOM, The FIRC Institute for Molecular Oncology
University of Milan, Medical School)
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.
Suggested Citation
Simona Polo & Sara Sigismund & Mario Faretta & Monica Guidi & Maria Rosaria Capua & Giovanna Bossi & Hong Chen & Pietro De Camilli & Pier Paolo Di Fiore, 2002.
"A single motif responsible for ubiquitin recognition and monoubiquitination in endocytic proteins,"
Nature, Nature, vol. 416(6879), pages 451-455, March.
Handle:
RePEc:nat:nature:v:416:y:2002:i:6879:d:10.1038_416451a
DOI: 10.1038/416451a
Download full text from publisher
As the access to this document is restricted, you may want to search for a different version of it.
Corrections
All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:nature:v:416:y:2002:i:6879:d:10.1038_416451a. See general information about how to correct material in RePEc.
If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.
We have no bibliographic references for this item. You can help adding them by using this form .
If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.
For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .
Please note that corrections may take a couple of weeks to filter through
the various RePEc services.