Acyl-CoA binding domain containing 3 (ACBD3) recruits the protein phosphatase PPM1L to ER-Golgi membrane contact sites |
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| Authors: | Yasuharu Shinoda Kohsuke Fujita Satoko Saito Hiroyuki Matsui Yusuke Kanto Yuko Nagaura Kohji Fukunaga Shinri Tamura Takayasu Kobayashi |
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| Institution: | a Department of Biochemistry, Institute of Development, Aging and Cancer, Tohoku University, Japan
b Department of Pharmacology, Graduate School of Pharmaceutical Sciences, Tohoku University, Japan |
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| Abstract: | The metal-dependent protein phosphatase family (PPM) governs a number of signaling pathways. PPM1L, originally identified as a negative regulator of stress-activated protein kinase signaling, was recently shown to be involved in the regulation of ceramide trafficking at ER-Golgi membrane contact sites. Here, we identified acyl-CoA binding domain containing 3 (ACBD3) as an interacting partner of PPM1L. We showed that this association, which recruits PPM1L to ER-Golgi membrane contact sites, is mediated by a GOLD (Golgi dynamics) domain in ACBD3. These results suggested that ACBD3 plays a pivotal role in ceramide transport regulation at the ER-Golgi interface.Structured summary of protein interactionsACBD3 and PPM1Lcolocalize by fluorescence microscopy (View interaction)FYCO1physically interacts with PPM1L by pull down (View interaction)SEC14L2physically interacts with PPM1L by pull down (View interaction)ACBD3physically interacts with PPM1L by pull down (View interaction)SEC14L1physically interacts with PPM1L by pull down (View interaction)PPM1Lphysically interacts with ACBD3 by two hybrid (View interaction) |
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| Keywords: | PPM1L metal-dependent protein phosphatase 1L ACBD3 acyl-CoA binding domain containing 3 ER endoplasmic reticulum GOLD Golgi dynamics FYCO1 FYVE and coiled-coil domain-containing protein 1 |
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