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Open Access Open Badges Research article

RNF122: A novel ubiquitin ligase associated with calcium-modulating cyclophilin ligand

Zhi Peng14, Taiping Shi123* and Dalong Ma123

Author Affiliations

1 Chinese National Human Genome Center, #3-707 North YongChang Road BDA, Beijing 100176, PR China

2 Laboratory of Medical Immunology, School of Basic Medical Science, Peking University Health Science Center, 38# Xueyuan Road, Beijing, 100191, PR China

3 Peking University Center for Human Disease Genomics, 38# Xueyuan Road, Beijing, 100191, PR China

4 Department of Medical Oncology, Yijishan Hospital, Wannan Medical College, Wuhu, Anhui, 241001, PR China

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BMC Cell Biology 2010, 11:41  doi:10.1186/1471-2121-11-41

Published: 17 June 2010



RNF122 is a recently discovered RING finger protein that is associated with HEK293T cell viability and is overexpressed in anaplastic thyroid cancer cells. RNF122 owns a RING finger domain in C terminus and transmembrane domain in N terminus. However, the biological mechanism underlying RNF122 action remains unknown.


In this study, we characterized RNF122 both biochemically and intracellularly in order to gain an understanding of its biological role. RNF122 was identified as a new ubiquitin ligase that can ubiquitinate itself and undergoes degradation in a RING finger-dependent manner. From a yeast two-hybrid screen, we identified calcium-modulating cyclophilin ligand (CAML) as an RNF122-interacting protein. To examine the interaction between CAML and RNF122, we performed co-immunoprecipitation and colocalization experiments using intact cells. What is more, we found that CAML is not a substrate of ubiquitin ligase RNF122, but that, instead, it stabilizes RNF122.


RNF122 can be characterized as a C3H2C3-type RING finger-containing E3 ubiquitin ligase localized to the ER. RNF122 promotes its own degradation in a RING finger-and proteasome-dependent manner. RNF122 interacts with CAML, and its E3 ubiquitin ligase activity was noted to be dependent on the RING finger domain.