Journal
JOURNAL OF CELL SCIENCE
Volume 127, Issue 22, Pages 4904-4917Publisher
COMPANY OF BIOLOGISTS LTD
DOI: 10.1242/jcs.155408
Keywords
Golgi; Microtubule; Myomegalin; Protein trafficking
Categories
Funding
- Research Grants Council of Hong Kong [662511, 662612, T13-607/12R]
- National Key Basic Research Program of China [2013CB530900]
- University Grants Committee of Hong Kong [AoE/M-06/08, SEG_HKUST05]
- Innovation and Technology Commission of Hong Kong [ITCPD/17-9]
- TUYF Charitable Trust [TUYF12SC05]
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The Golgi of mammalian cells is known to be a major microtubule-organizing site that requires microtubules for its organization and protein trafficking. However, the mechanisms underlying the microtubule organization of the Golgi remain obscure. We used immunoprecipitation coupled with mass spectrometry to identify a widely expressed isoform of the poorly characterized muscle protein myomegalin. This newly identified isoform, myomegalin variant 8 (MMG8), localized predominantly to cis-Golgi networks by interacting with AKAP450 (also known as AKAP9), and this interaction with AKAP450 was required for the stability of both proteins. Disrupting MMG8 expression affected endoplasmic reticulum (ER)-to-Golgi trafficking and caused Golgi fragmentation. Furthermore, MMG8 associated with c-tubulin complexes and with the microtubule plus-end tracking protein EB1 (also known as MAPRE1), and was required for the Golgi localization of these two molecules. On the Golgi, c-tubulin complexes mediated microtubule nucleation, whereas EB1 functioned in ER-to-Golgi trafficking. These results indicate that MMG8 participates in Golgi microtubule organization and thereby plays a crucial role in the organization and function of the Golgi.
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