PML protein isoforms and the RBCC/TRIM motif. Export

@article{citeulike:510646, abstract = {PML is a component of a multiprotein complex, termed nuclear bodies, and the PML protein was originally discovered in patients suffering from acute promyelocytic leukaemia (APL). APL is associated with a reciprocal chromosomal translocation of chromosomes 15 and 17, which results in a fusion protein comprising PML and the retinoic acid receptor alpha. The PML genomic locus is approximately 35 kb and is subdivided into nine exons. A large number of alternative spliced transcripts are synthesized from the PML gene, resulting in a variety of PML proteins ranging in molecular weight from 48-97 kDa. In this review we summarize the data on the known PML isoforms and splice variants and present a new unifying nomenclature. Although, the function/s of the PML variants are unclear, all PML isoforms contain an identical N-terminal region, suggesting that these sequences are indispensable for function, but differ in their C-terminal sequences. The N-terminal region harbours a RING-finger, two B-boxes and a predicted alpha-helical Coiled-Coil domain, that together form the RBCC/TRIM motif found in a large family of proteins. In PML this motif is essential for PML nuclear body formation in vivo and PML-homo and hetero interactions conferring growth suppressor, apoptotic and anti-viral activities. In APL oligomerization mediated by the RBCC/TRIM motif is essential for the transformation potential of the PML-RARalpha fusion protein.}, address = {Centre for Structural Biology, Imperial College of Science, Technology and Medicine, Flowers Building, Armstrong Road, London SW7 2AZ, UK.}, author = {Jensen, K. and Shiels, C. and Freemont, P. S.}, citeulike-article-id = {510646}, citeulike-linkout-0 = {http://view.ncbi.nlm.nih.gov/pubmed/11704850}, citeulike-linkout-1 = {http://www.hubmed.org/display.cgi?uids=11704850}, day = {29}, issn = {0950-9232}, journal = {Oncogene}, keywords = {domain, ring}, month = {October}, number = {49}, pages = {7223--7233}, posted-at = {2006-02-18 16:18:58}, priority = {2}, title = {PML protein isoforms and the RBCC/TRIM motif.}, url = {http://view.ncbi.nlm.nih.gov/pubmed/11704850}, volume = {20}, year = {2001} }

TY - JOUR ID - citeulike:510646 L3 - citeulike-article-id:510646 N2 - PML is a component of a multiprotein complex, termed nuclear bodies, and the PML protein was originally discovered in patients suffering from acute promyelocytic leukaemia (APL). APL is associated with a reciprocal chromosomal translocation of chromosomes 15 and 17, which results in a fusion protein comprising PML and the retinoic acid receptor alpha. The PML genomic locus is approximately 35 kb and is subdivided into nine exons. A large number of alternative spliced transcripts are synthesized from the PML gene, resulting in a variety of PML proteins ranging in molecular weight from 48-97 kDa. In this review we summarize the data on the known PML isoforms and splice variants and present a new unifying nomenclature. Although, the function/s of the PML variants are unclear, all PML isoforms contain an identical N-terminal region, suggesting that these sequences are indispensable for function, but differ in their C-terminal sequences. The N-terminal region harbours a RING-finger, two B-boxes and a predicted alpha-helical Coiled-Coil domain, that together form the RBCC/TRIM motif found in a large family of proteins. In PML this motif is essential for PML nuclear body formation in vivo and PML-homo and hetero interactions conferring growth suppressor, apoptotic and anti-viral activities. In APL oligomerization mediated by the RBCC/TRIM motif is essential for the transformation potential of the PML-RARalpha fusion protein. IS - 49 JF - Oncogene SN - 0950-9232 AD - Centre for Structural Biology, Imperial College of Science, Technology and Medicine, Flowers Building, Armstrong Road, London SW7 2AZ, UK. EP - 7233 TI - PML protein isoforms and the RBCC/TRIM motif. VL - 20 SP - 7223 KW - domain KW - ring AU - Jensen, K AU - Shiels, C AU - Freemont, PS PY - 2001/10/29/ UR - http://view.ncbi.nlm.nih.gov/pubmed/11704850 ER -