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- Title
The absence of Rab27a accelerates the degradation of Melanophilin.
- Authors
Park, Jong il; Lee, Ji Eun; Myung, Cheol hwan; Jo, Chan song; Jang, Hye Sung; Hwang, Jae Sung
- Abstract
Melanophilin (Mlph) forms an interaction with Rab27a and the actin‐based motor protein MyosinVa (MyoVa) on mature melanosome membranes and the tripartite complex regulates melanosome transport in melanocytes. In this study, we found that Rab27a siRNA decreased Mlph and Rab27a protein levels, but Mlph mRNA levels were not changed. Other Rab27a siRNA sequences also showed the same results. When Rab27a siRNA was treated with melan‐a melanocytes, Rab27a protein was decreased within 6 hours and Mlph protein was decreased within 24 hours. To determine whether the absence of Rab27a promotes Mlph degradation, we inhibited protein degradation by treatment with proteasome (MG132) and lysosomal enzyme (E64D and Pepstatin A) inhibitors in melan‐a melanocytes. MG132 inhibited the degradation of Mlph, but E64D and Pepstatin A had no effect on Mlph. The absence of Rab27a enhanced ubiquitination of Mlph and induced proteasomal degradation. From these results, we concluded that Mlph interaction with Rab27a is important for Mlph stability and melanosome transport.
- Subjects
PROTEOLYSIS; MOLECULAR motor proteins; MELANOCYTES; SMALL interfering RNA; UBIQUITINATION; MESSENGER RNA
- Publication
Experimental Dermatology, 2019, Vol 28, Issue 1, p90
- ISSN
0906-6705
- Publication type
Article
- DOI
10.1111/exd.13840