Effects of carboxyl methylation of photoreceptor G protein gamma-subunit in visual transduction.

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書誌事項

公開日
1994-02
権利情報
  • https://www.elsevier.com/tdm/userlicense/1.0/
  • https://www.elsevier.com/legal/tdmrep-license
  • http://creativecommons.org/licenses/by/4.0/
DOI
  • 10.1016/s0021-9258(17)37670-6
公開者
Elsevier BV

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説明

G protein gamma-subunits are isoprenylated and carboxyl-methylated at the C-terminal cysteine, which is indispensable for the function of photoreceptor G protein transducin (T alpha beta gamma). However, the physiological role of the methylation and its reversibility have been unclear. Here we isolated methylated and non-methylated forms of farnesylated T beta gamma, and demonstrated that the methylation remarkably facilitates not only the membrane association of T beta gamma but also the subunit interaction between T alpha and T beta gamma. Consequently, the functional coupling of transducin with light-activated receptor, metarhodopsin II, was stabilized by the methylation, resulting in acceleration of GTP gamma S (guanosine 5'-3-O-(thio) triphosphate) binding to T alpha. An examination of the reversibility of the methylation suggested that T gamma is kept fully methylated in rod outer segments. These observations indicate that the methylation of T gamma plays an important role in the most efficient photon-signal transduction process in rod cells.

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