2018
DOI: 10.1111/tra.12554
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Sac1, a lipid phosphatase at the interface of vesicular and nonvesicular transport

Abstract: The lipid phosphatase Sac1 dephosphorylates phosphatidylinositol 4-phosphate (PI4P), thereby holding levels of this crucial membrane signaling molecule in check. Sac1 regulates multiple cellular processes, including cytoskeletal organization, membrane trafficking and cell signaling. Here, we review the structure and regulation of Sac1, its roles in cell signaling and development and its links to health and disease. Remarkably, many of the diverse roles attributed to Sac1 can be explained by the recent discover… Show more

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Cited by 59 publications
(49 citation statements)
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References 211 publications
(698 reference statements)
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“…The second crucial result of our work is that CPT1C regulates GluA1 trafficking through SAC1-dependent modulation of TGN PI(4)P levels. To our knowledge, this is the first report of a negative regulator of SAC1 enzymatic activity (for an exhaustive review on SAC1, see Del Bel and Brill, 2018). SAC1 PI(4)P phosphatase activity assays in cell lines and brain tissues demonstrate that SAC1 activity is regulated by CPT1C in an energy-dependent manner.…”
Section: Discussionmentioning
confidence: 82%
See 1 more Smart Citation
“…The second crucial result of our work is that CPT1C regulates GluA1 trafficking through SAC1-dependent modulation of TGN PI(4)P levels. To our knowledge, this is the first report of a negative regulator of SAC1 enzymatic activity (for an exhaustive review on SAC1, see Del Bel and Brill, 2018). SAC1 PI(4)P phosphatase activity assays in cell lines and brain tissues demonstrate that SAC1 activity is regulated by CPT1C in an energy-dependent manner.…”
Section: Discussionmentioning
confidence: 82%
“…As mentioned above, CPT1C regulates PI(4)P levels in the TGN compartment. This finding can be explained by the involvement of the TGN lipid phosphatase SAC1, which is a strong regulator of PI(4)P (reviewed by Del Bel and Brill, 2018) and has been reported to interact with CPT1C (Brechet et al, 2017). Thus, we explored a potential role for malonyl-CoA sensing and the CPT1C C-terminus in tuning CPT1C-SAC1 interactions.…”
Section: Characterization Of Cpt1c-sac1 Interactionmentioning
confidence: 99%
“…In particular, PtdIns delivered from the ER can be rapidly phosphorylated within the PM by the PI4KA complex to locally produce PtdIns4P. At the same time, the levels of PtdIns4P within the ER are normally kept extremely low because of the activity of the ER‐resident phosphatase, suppressor of actin mutations 1‐like (Sac1), which selectively dephosphorylates PtdIns4P to produce PtdIns . The combined activities of PI4KA and Sac1 therefore function to establish a PtdIns4P gradient between the PM and ER that can be used to inform the directional movement of lipids at ER‐PM contacts (Figure ).…”
Section: Phosphatidylinositol 4‐phosphate Gradients and Non‐vesicularmentioning
confidence: 99%
“…The non-abundant PI5P phosphoinositide is related to the Akt kinase pathway and relevant for several cellular processes, such as survival and cell growth, with a prominent role in cancer [66]. Hydrolysis of phosphatidylinositol 3-phosphate (PI3P), phosphatidylinositol 4-phosphate (PI4P), and phosphatidylinositol 3,5-bisphosphate(PI(3,5)P2) is carried out by SACM1L/Sac1, which is enriched at the Golgi membrane, but is also present in ER membranes [67]. The preferential substrate for this enzyme is PI4P.…”
Section: Understanding Channel Trafficking Through Protein-protein Inmentioning
confidence: 99%