Abstract:
:Human uncoupling protein 3 (UCP3) has two RNA transcripts that arise from the differential processing of the same gene product. One encodes the full length protein (UCP3L) while the other encodes a truncated version (UCP3S) lacking the sixth membrane spanning domain. The roles of the two isoforms are not known, but a mutation that decreases the proportion of UCP3L decreases fat oxidation and increases susceptibility to obesity. In the ADP/ATP carrier, a protein closely related to UCP3, the sixth membrane spanning domain is required for insertion into the inner membrane. Therefore, defective membrane insertion of UCP3S may account for the different effects of the two isoforms in vivo. We investigated mitochondrial import of the two UCP3 isoforms. When epitope-tagged versions of UCP3S and UCP3L were expressed in COS7 cells, both were inserted into the mitochondrial inner membrane. Translation in vitro followed by incubation with isolated mitochondria showed that both isoforms were inserted into the inner membrane, however, the insertion of UCP3S was significantly slower.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Renold A,Koehler CM,Murphy MPdoi
10.1016/s0014-5793(99)01688-9keywords:
subject
Has Abstractpub_date
2000-01-14 00:00:00pages
135-40issue
2-3eissn
0014-5793issn
1873-3468pii
S0014-5793(99)01688-9journal_volume
465pub_type
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