The SUN2-nesprin-2 LINC complex and KIF20A function in the Golgi dispersal.

Affiliation

Hieda M(1)(2), Matsumoto T(3), Isobe M(4)(5), Kurono S(6)(7), Yuka K(6)(7), Kametaka S(4), Wang JY(8), Chi YH(8), Kameda K(9), Kimura H(10), Matsuura N(6)(11), Matsuura S(6).
Author information:
(1)Graduate School of Health Sciences, Ehime Prefectural University of Health Sciences, Ehime, 791-2101, Japan. [Email]
(2)Graduate School of Medicine and Health Science, Osaka University, Osaka, 565-0871, Japan. [Email]
(3)Graduate School of Health Sciences, Ehime Prefectural University of Health Sciences, Ehime, 791-2101, Japan.
(4)Nagoya University Graduate School of Medicine, Nagoya, 461-0047, Japan.
(5)Graduate School of Medicine and Dental Sciences, Kagoshima University, Kagoshima, 890-8544, Japan.
(6)Graduate School of Medicine and Health Science, Osaka University, Osaka, 565-0871, Japan.
(7)Laboratory Chemicals Division, Wako Pure Chemical Industries, Ltd, Osaka, 540-8605, Japan.
(8)Institute of Biotechnology and Pharmaceutical Research, National Health Research Institutes, Zhunan Township, Taiwan.
(9)ADRES, Ehime University, Ehime, 791-0204, Japan.
(10)Institute of Innovative Research, Tokyo Institute of Technology, Yokohama, 226-8501, Japan.
(11)Osaka International Cancer Institute, Osaka, 541-8567, Japan.

Abstract

The morphology of the Golgi complex is influenced by the cellular context, which strictly correlates with nuclear functions; however, the mechanism underlying this association remains elusive. The inner nuclear membrane SUN proteins, SUN1 and SUN2, have diverse functions together with the outer nuclear membrane nesprin proteins, which comprise the LINC complex. We found that depletion of SUN1 leads to Golgi complex dispersion with maintenance of ministacks and retained function for vesicle transport through the Golgi complex. In addition, SUN2 associates with microtubule plus-end-directed motor KIF20A, possibly via nesprin-2. KIF20A plays a role in the Golgi dispersion in conjunction with the SUN2-nesprin-2 LINC complex in SUN1-depleted cells, suggesting that SUN1 suppresses the function of the SUN2-nesprin-2 LINC complex under a steady-state condition. Further, SUN1-knockout mice, which show impaired cerebellar development and cerebellar ataxia, presented altered Golgi morphology in Purkinje cells. These findings revealed a regulation of the Golgi organization by the LINC complex.