The Ubiquitin-conjugating Enzymes UbcH7 and UbcH8 Interact with RING Finger/IBR Motif-containing Domains of HHARI and H7-AP1

Moynihan, Terry P.; Ardley, Helen C.; Nuber, Ulrike; Rose, Stephen A.; Jones, Pamela F.; Markham, Alexander F.; Scheffner, Martin; Robinson, Philip A.

The Ubiquitin-conjugating Enzymes UbcH7 and UbcH8 Interact with RING Finger/IBR Motif-containing Domains of HHARI and H7-AP1

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Datum

1999

Autor:innen

Moynihan, Terry P.

Ardley, Helen C.

Nuber, Ulrike

Rose, Stephen A.

Jones, Pamela F.

Markham, Alexander F.

Scheffner, Martin

Robinson, Philip A.

DOI (zitierfähiger Link)

10.1074/jbc.274.43.30963

Sammlungen

Biologie

Publikationstyp

Zeitschriftenartikel

Publikationsstatus

Published

Erschienen in

The Journal of Biological Chemistry : JBC ; 274 (1999), 43. - S. 30963-30968. - ISSN 0021-9258. - eISSN 1083-351X

Zusammenfassung

Ubiquitinylation of proteins appears to be mediated by the specific interplay between ubiquitin-conjugating enzymes (E2s) and ubiquitin-protein ligases (E3s). However, cognate E3s and/or substrate proteins have been identified for only a few E2s. To identify proteins that can interact with the human E2 UbcH7, a yeast two-hybrid screen was performed. Two proteins were identified and termed human homologue of Drosophila ariadne (HHARI) and UbcH7-associated protein (H7-AP1). Both proteins, which are widely expressed, are characterized by the presence of RING finger and in between RING fingers (IBR) domains. No other overt structural similarity was observed between the two proteins. In vitrobinding studies revealed that an N-terminal RING finger motif (HHARI) and the IBR domain (HHARI and H7-AP1) are involved in the interaction of these proteins with UbcH7. Furthermore, binding of these two proteins to UbcH7 is specific insofar that both HHARI and H7-AP1 can bind to the closely related E2, UbcH8, but not to the unrelated E2s UbcH5 and UbcH1. Although it is not clear at present whether HHARI and H7-AP1 serve, for instance, as substrates for UbcH7 or represent proteins with E3 activity, our data suggests that a subset of RING finger/IBR proteins are functionally linked to the ubiquitin/proteasome pathway.

Fachgebiet (DDC)

570 Biowissenschaften, Biologie

Zitieren

ISO 690

MOYNIHAN, Terry P., Helen C. ARDLEY, Ulrike NUBER, Stephen A. ROSE, Pamela F. JONES, Alexander F. MARKHAM, Martin SCHEFFNER, Philip A. ROBINSON, 1999. The Ubiquitin-conjugating Enzymes UbcH7 and UbcH8 Interact with RING Finger/IBR Motif-containing Domains of HHARI and H7-AP1. In: The Journal of Biological Chemistry : JBC. 274(43), pp. 30963-30968. ISSN 0021-9258. eISSN 1083-351X. Available under: doi: 10.1074/jbc.274.43.30963

BibTex

@article{Moynihan1999-10-22Ubiqu-42655,
  year={1999},
  doi={10.1074/jbc.274.43.30963},
  title={The Ubiquitin-conjugating Enzymes UbcH7 and UbcH8 Interact with RING Finger/IBR Motif-containing Domains of HHARI and H7-AP1},
  number={43},
  volume={274},
  issn={0021-9258},
  journal={The Journal of Biological Chemistry : JBC},
  pages={30963--30968},
  author={Moynihan, Terry P. and Ardley, Helen C. and Nuber, Ulrike and Rose, Stephen A. and Jones, Pamela F. and Markham, Alexander F. and Scheffner, Martin and Robinson, Philip A.}
}

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