SPRING is a Dedicated Licensing Factor for SREBP-Specific Activation by S1P

SREBP transcription factors are central regulators of lipid metabolism. Their proteolytic activation requires ER to the Golgi translocation and subsequent cleavage by site-1-protease (S1P). Produced as a proprotein, S1P undergoes autocatalytic cleavage from its precursor S1P to mature S1P form. Here...

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Veröffentlicht in:	Molecular and cellular biology Jg. 44; H. 4; S. 123 - 137
Hauptverfasser:	Hendrix, Sebastian, Tan, Josephine M. E., Ndoj, Klevis, Kingma, Jenina, Valiloo, Masoud, Zijlstra, Lobke F., Ottenhoff, Roelof, Seidah, Nabil G., Loregger, Anke, Kober, Daniel L., Zelcer, Noam
Format:	Journal Article
Sprache:	Englisch
Veröffentlicht:	United States Taylor & Francis 2024
Schlagworte:	Animals Cell Biology Endoplasmic Reticulum - metabolism Golgi Apparatus - metabolism HEK293 Cells Humans Liver - metabolism Mice Mice, Knockout Proprotein Convertases - genetics Proprotein Convertases - metabolism Proteolysis Serine Endopeptidases - genetics Serine Endopeptidases - metabolism Signal Transduction Sterol Regulatory Element Binding Proteins - genetics Sterol Regulatory Element Binding Proteins - metabolism SPRING S1P SREBP proteolytic enzyme C12ORF49 cholesterol regulation post-transcriptional regulation lipid metabolism Cholesterol metabolism proteolysis
ISSN:	1098-5549, 0270-7306, 1098-5549
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Abstract	SREBP transcription factors are central regulators of lipid metabolism. Their proteolytic activation requires ER to the Golgi translocation and subsequent cleavage by site-1-protease (S1P). Produced as a proprotein, S1P undergoes autocatalytic cleavage from its precursor S1P to mature S1P form. Here, we report that SPRING (previously C12ORF29) and S1P interact through their ectodomains, and that this facilitates the autocatalytic cleavage of S1P into its mature S1P form. Reciprocally, we identified a S1P recognition-motif in SPRING and demonstrate that S1P-mediated cleavage leads to secretion of the SPRING ectodomain in cells, and in liver-specific knockout (LKO) mice transduced with AAV-mSpring. By reconstituting SPRING variants into SPRING cells we show that the SPRING ectodomain supports proteolytic maturation of S1P and SREBP signaling, but that S1P-mediated SPRING cleavage is not essential for these processes. Absence of SPRING modestly diminishes proteolytic maturation of S1P and trafficking of S1P to the Golgi. However, despite reaching the Golgi in SPRING cells, S1P fails to rescue SREBP signaling. Remarkably, whereas SREBP signaling was severely attenuated in SPRING cells and LKO mice, that of ATF6, another S1P substrate, was unaffected in these models. Collectively, our study positions SPRING as a dedicated licensing factor for SREBP-specific activation by S1P.
AbstractList	SREBP transcription factors are central regulators of lipid metabolism. Their proteolytic activation requires ER to the Golgi translocation and subsequent cleavage by site-1-protease (S1P). Produced as a proprotein, S1P undergoes autocatalytic cleavage from its precursor S1P to mature S1P form. Here, we report that SPRING (previously C12ORF29) and S1P interact through their ectodomains, and that this facilitates the autocatalytic cleavage of S1P into its mature S1P form. Reciprocally, we identified a S1P recognition-motif in SPRING and demonstrate that S1P-mediated cleavage leads to secretion of the SPRING ectodomain in cells, and in liver-specific knockout (LKO) mice transduced with AAV-mSpring. By reconstituting SPRING variants into SPRING cells we show that the SPRING ectodomain supports proteolytic maturation of S1P and SREBP signaling, but that S1P-mediated SPRING cleavage is not essential for these processes. Absence of SPRING modestly diminishes proteolytic maturation of S1P and trafficking of S1P to the Golgi. However, despite reaching the Golgi in SPRING cells, S1P fails to rescue SREBP signaling. Remarkably, whereas SREBP signaling was severely attenuated in SPRING cells and LKO mice, that of ATF6, another S1P substrate, was unaffected in these models. Collectively, our study positions SPRING as a dedicated licensing factor for SREBP-specific activation by S1P. SREBP transcription factors are central regulators of lipid metabolism. Their proteolytic activation requires ER to the Golgi translocation and subsequent cleavage by site-1-protease (S1P). Produced as a proprotein, S1P undergoes autocatalytic cleavage from its precursor S1PA to mature S1PC form. Here, we report that SPRING (previously C12ORF29) and S1P interact through their ectodomains, and that this facilitates the autocatalytic cleavage of S1PA into its mature S1PC form. Reciprocally, we identified a S1P recognition-motif in SPRING and demonstrate that S1P-mediated cleavage leads to secretion of the SPRING ectodomain in cells, and in liver-specific Spring knockout (LKO) mice transduced with AAV-mSpring. By reconstituting SPRING variants into SPRINGKO cells we show that the SPRING ectodomain supports proteolytic maturation of S1P and SREBP signaling, but that S1P-mediated SPRING cleavage is not essential for these processes. Absence of SPRING modestly diminishes proteolytic maturation of S1PA→C and trafficking of S1PC to the Golgi. However, despite reaching the Golgi in SPRINGKO cells, S1PC fails to rescue SREBP signaling. Remarkably, whereas SREBP signaling was severely attenuated in SPRINGKO cells and LKO mice, that of ATF6, another S1P substrate, was unaffected in these models. Collectively, our study positions SPRING as a dedicated licensing factor for SREBP-specific activation by S1P.SREBP transcription factors are central regulators of lipid metabolism. Their proteolytic activation requires ER to the Golgi translocation and subsequent cleavage by site-1-protease (S1P). Produced as a proprotein, S1P undergoes autocatalytic cleavage from its precursor S1PA to mature S1PC form. Here, we report that SPRING (previously C12ORF29) and S1P interact through their ectodomains, and that this facilitates the autocatalytic cleavage of S1PA into its mature S1PC form. Reciprocally, we identified a S1P recognition-motif in SPRING and demonstrate that S1P-mediated cleavage leads to secretion of the SPRING ectodomain in cells, and in liver-specific Spring knockout (LKO) mice transduced with AAV-mSpring. By reconstituting SPRING variants into SPRINGKO cells we show that the SPRING ectodomain supports proteolytic maturation of S1P and SREBP signaling, but that S1P-mediated SPRING cleavage is not essential for these processes. Absence of SPRING modestly diminishes proteolytic maturation of S1PA→C and trafficking of S1PC to the Golgi. However, despite reaching the Golgi in SPRINGKO cells, S1PC fails to rescue SREBP signaling. Remarkably, whereas SREBP signaling was severely attenuated in SPRINGKO cells and LKO mice, that of ATF6, another S1P substrate, was unaffected in these models. Collectively, our study positions SPRING as a dedicated licensing factor for SREBP-specific activation by S1P. SREBP transcription factors are central regulators of lipid metabolism. Their proteolytic activation requires ER to the Golgi translocation and subsequent cleavage by site-1-protease (S1P). Produced as a proprotein, S1P undergoes autocatalytic cleavage from its precursor S1PA to mature S1PC form. Here, we report that SPRING (previously C12ORF29) and S1P interact through their ectodomains, and that this facilitates the autocatalytic cleavage of S1PA into its mature S1PC form. Reciprocally, we identified a S1P recognition-motif in SPRING and demonstrate that S1P-mediated cleavage leads to secretion of the SPRING ectodomain in cells, and in liver-specific Spring knockout (LKO) mice transduced with AAV-mSpring. By reconstituting SPRING variants into SPRINGKO cells we show that the SPRING ectodomain supports proteolytic maturation of S1P and SREBP signaling, but that S1P-mediated SPRING cleavage is not essential for these processes. Absence of SPRING modestly diminishes proteolytic maturation of S1PA→C and trafficking of S1PC to the Golgi. However, despite reaching the Golgi in SPRINGKO cells, S1PC fails to rescue SREBP signaling. Remarkably, whereas SREBP signaling was severely attenuated in SPRINGKO cells and LKO mice, that of ATF6, another S1P substrate, was unaffected in these models. Collectively, our study positions SPRING as a dedicated licensing factor for SREBP-specific activation by S1P.
Author	Kingma, Jenina Zijlstra, Lobke F. Ottenhoff, Roelof Valiloo, Masoud Loregger, Anke Zelcer, Noam Tan, Josephine M. E. Ndoj, Klevis Seidah, Nabil G. Kober, Daniel L. Hendrix, Sebastian
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Keywords	SPRING S1P SREBP proteolytic enzyme C12ORF49 cholesterol regulation post-transcriptional regulation lipid metabolism Cholesterol metabolism proteolysis
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Notes	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 Current affiliation: Institute for Diabetes, Obesity & Metabolism, Department of Cell and Developmental Biology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania 19104 USA Current affiliation: Myllia Biotechnology GmbH, Am Kanal 27, 1110 Vienna, Austria Supplemental data for this article can be accessed online at https://doi.org/10.1080/10985549.2024.2348711.
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SubjectTerms	Animals Cell Biology Endoplasmic Reticulum - metabolism Golgi Apparatus - metabolism HEK293 Cells Humans Liver - metabolism Mice Mice, Knockout Proprotein Convertases - genetics Proprotein Convertases - metabolism Proteolysis Serine Endopeptidases - genetics Serine Endopeptidases - metabolism Signal Transduction Sterol Regulatory Element Binding Proteins - genetics Sterol Regulatory Element Binding Proteins - metabolism
Title	SPRING is a Dedicated Licensing Factor for SREBP-Specific Activation by S1P
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