The cytoplasmic AID complex.
Although AID fulfils its physiological function of diversifying antibody genes in the nucleus, most of the AID protein within the cell is found in a complex located in the cytoplasm. In this review, we summarize what is currently known about this cytoplasmic AID complex. Its size has been estimated to lie between 300 and 500kDa (sedimentation coefficient of 10-11S) and it comprises the abundant protein translation elongation factor 1α (eEF1A) as a major stoichiometric component. We speculate on the possible roles of this complex as well as of chaperones known to interact with AID in regulating the cytosolic retention of AID and its controlled release for import into the nucleus.
Medical Research Council Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QH, UK. julien.hasler@gmail.com
Julien
J
Häsler
Cristina
C
Rada
Michael S
MS
Neuberger
D000818:Animals; D003564:Cytidine Deaminase / Q000276:immunology / Q000378:metabolism*; D003593:Cytoplasm / Q000276:immunology / Q000378:metabolism*; D006801:Humans; D011485:Protein Binding; D055503:Protein Multimerization; D012313:RNA / Q000378:metabolism; D000098830:AICDA (Activation-Induced Cytidine Deaminase)
D012313:RNA; D000098830:AICDA (Activation-Induced Cytidine Deaminase); D003564:Cytidine Deaminase