RN181, a novel ubiquitin E3 ligase that interacts with the KVGFFKR motif of platelet integrin alpha(IIb)beta3

We previously identified proteins that bind with high affinity to a peptide corresponding to the cytoplasmic regulatory domain (KVGFFKR) of the platelet-specific integrin subunit alpha(IIb). These included a hypothetical protein termed HSPC238, recently renamed as RING finger protein, RN181. Here, w...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 2008-05, Vol.369 (4), p.1088-1093
Main Authors: Brophy, Teresa M, Raab, Markus, Daxecker, Heide, Culligan, Kevin G, Lehmann, Ingo, Chubb, Anthony J, Treumann, Achim, Moran, Niamh
Format: Article
Language:English
Subjects:
Amino Acid Motifs
Amino Acid Sequence
Blood Platelets - enzymology
Blood Platelets - metabolism
Calcium - metabolism
Conserved Sequence
Humans
Models, Molecular
Molecular Sequence Data
Platelet Glycoprotein GPIIb-IIIa Complex - chemistry
Platelet Glycoprotein GPIIb-IIIa Complex - metabolism
Protein Structure, Tertiary
RNA, Messenger - analysis
RNA, Messenger - metabolism
Ubiquitin-Protein Ligases - chemistry
Ubiquitin-Protein Ligases - genetics
Ubiquitin-Protein Ligases - metabolism
Ubiquitination
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Summary:We previously identified proteins that bind with high affinity to a peptide corresponding to the cytoplasmic regulatory domain (KVGFFKR) of the platelet-specific integrin subunit alpha(IIb). These included a hypothetical protein termed HSPC238, recently renamed as RING finger protein, RN181. Here, we establish the presence of RN181 in human platelets by RT-PCR, Western blotting and mass spectrometry and confirm its affinity for the platelet integrin. We demonstrate that RN181 has ubiquitin E3 ligase activity and that all other components of the ubiquitination pathway are abundant in platelets, suggesting a novel link of integrin signal transduction pathways with ubiquitin-conjugation events.
ISSN:1090-2104
DOI:10.1016/j.bbrc.2008.02.142