Acyl-CoA binding domain containing 3 (ACBD3) recruits the protein phosphatase PPM1L to ER–Golgi membrane contact sites

► Acyl-CoA binding domain containing 3 (ACBD3) is an interacting partner of PPM1L. ► This association is mediated by a GOLD (Golgi dynamics) domain in ACBD3. ► ACBD3 recruits PPM1L to ER–Golgi membrane contact sites. ► ACBD3 plays a pivotal role in ceramide transport regulation. The metal-dependent...

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Veröffentlicht in:FEBS letters 2012-09, Vol.586 (19), p.3024-3029
Hauptverfasser: Shinoda, Yasuharu, Fujita, Kohsuke, Saito, Satoko, Matsui, Hiroyuki, Kanto, Yusuke, Nagaura, Yuko, Fukunaga, Kohji, Tamura, Shinri, Kobayashi, Takayasu
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Sprache:eng
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Zusammenfassung:► Acyl-CoA binding domain containing 3 (ACBD3) is an interacting partner of PPM1L. ► This association is mediated by a GOLD (Golgi dynamics) domain in ACBD3. ► ACBD3 recruits PPM1L to ER–Golgi membrane contact sites. ► ACBD3 plays a pivotal role in ceramide transport regulation. 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. ACBD3 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)
ISSN:0014-5793
1873-3468
DOI:10.1016/j.febslet.2012.06.050