RN181, a novel ubiquitin E3 ligase that interacts with the KVGFFKR motif of platelet integrin α_IIbβ₃

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• 作者：Teresa M. Brophy ; Markus Raab ; Heide Daxecker ; Kevin G. Culligan ; Ingo Lehmann ; Anthony J. Chubb ; Achim Treumann ; Niamh Moran
• 关键词：Integrin ; Platelet ; RN181 ; Ubiquitin E3 ligase
• 刊名：Biochemical and Biophysical Research Communications
• 出版年：2008
• 出版时间：16 May 2008
• 年：2008
• 卷：369
• 期：4
• 页码：1088-1093
• 全文大小：538 K

文摘

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 _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.