SPRING licenses S1P-mediated cleavage of SREBP2 by displacing an inhibitory pro-domain

Site-one protease (S1P) conducts the first of two cleavage events in the Golgi to activate Sterol regulatory element binding proteins (SREBPs) and upregulate lipogenic transcription. S1P is also required for a wide array of additional signaling pathways. A zymogen serine protease, S1P matures throug...

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Published in:Nature communications Vol. 15; no. 1; pp. 5732 - 17
Main Authors: Hendrix, Sebastian, Dartigue, Vincent, Hall, Hailee, Bawaria, Shrankhla, Kingma, Jenina, Bajaj, Bilkish, Zelcer, Noam, Kober, Daniel L.
Format: Journal Article
Language:English
Published: London Nature Publishing Group UK 09.07.2024
Nature Publishing Group
Nature Portfolio
Subjects:
101/28
13/106
13/109
631/45/287/1197
631/45/468
631/45/535/1258/1259
82/29
82/83
Animals
Biochemistry
Cholesterol
Cholesterol - metabolism
Cleavage
Cryoelectron Microscopy
Endoplasmic reticulum
Endoplasmic Reticulum - metabolism
Enzymes
Fatty acids
Golgi apparatus
Golgi Apparatus - metabolism
HEK293 Cells
Homeostasis
Humanities and Social Sciences
Humans
Licenses
Metabolism
multidisciplinary
Mutation
Peptides
Proenzymes
Proprotein Convertases - genetics
Proprotein Convertases - metabolism
Protease
Protein Domains
Regulatory sequences
Science
Science (multidisciplinary)
Serine Endopeptidases - chemistry
Serine Endopeptidases - genetics
Serine Endopeptidases - metabolism
Serine proteinase
Signal Transduction
Sterol Regulatory Element Binding Protein 2 - genetics
Sterol Regulatory Element Binding Protein 2 - metabolism
Sterol regulatory element-binding protein
Sterols
Substrates
Transcription factors
ISSN:2041-1723, 2041-1723
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Abstract Site-one protease (S1P) conducts the first of two cleavage events in the Golgi to activate Sterol regulatory element binding proteins (SREBPs) and upregulate lipogenic transcription. S1P is also required for a wide array of additional signaling pathways. A zymogen serine protease, S1P matures through autoproteolysis of two pro-domains, with one cleavage event in the endoplasmic reticulum (ER) and the other in the Golgi. We recently identified the SREBP regulating gene, (SPRING), which enhances S1P maturation and is necessary for SREBP signaling. Here, we report the cryo-EM structures of S1P and S1P-SPRING at sub-2.5 Å resolution. SPRING activates S1P by dislodging its inhibitory pro-domain and stabilizing intra-domain contacts. Functionally, SPRING licenses S1P to cleave its cognate substrate, SREBP2. Our findings reveal an activation mechanism for S1P and provide insights into how spatial control of S1P activity underpins cholesterol homeostasis. The authors report the structural basis of site-one protease (S1P) activation by SREBP regulating gene (SPRING). They show that SPRING displaces the inhibitory pro-domain of S1P, enabling S1P to cleave its canonical substrate SREBP2.
AbstractList Site-one protease (S1P) conducts the first of two cleavage events in the Golgi to activate Sterol regulatory element binding proteins (SREBPs) and upregulate lipogenic transcription. S1P is also required for a wide array of additional signaling pathways. A zymogen serine protease, S1P matures through autoproteolysis of two pro-domains, with one cleavage event in the endoplasmic reticulum (ER) and the other in the Golgi. We recently identified the SREBP regulating gene, (SPRING), which enhances S1P maturation and is necessary for SREBP signaling. Here, we report the cryo-EM structures of S1P and S1P-SPRING at sub-2.5 Å resolution. SPRING activates S1P by dislodging its inhibitory pro-domain and stabilizing intra-domain contacts. Functionally, SPRING licenses S1P to cleave its cognate substrate, SREBP2. Our findings reveal an activation mechanism for S1P and provide insights into how spatial control of S1P activity underpins cholesterol homeostasis.
Site-one protease (S1P) conducts the first of two cleavage events in the Golgi to activate Sterol regulatory element binding proteins (SREBPs) and upregulate lipogenic transcription. S1P is also required for a wide array of additional signaling pathways. A zymogen serine protease, S1P matures through autoproteolysis of two pro-domains, with one cleavage event in the endoplasmic reticulum (ER) and the other in the Golgi. We recently identified the SREBP regulating gene, (SPRING), which enhances S1P maturation and is necessary for SREBP signaling. Here, we report the cryo-EM structures of S1P and S1P-SPRING at sub-2.5 Å resolution. SPRING activates S1P by dislodging its inhibitory pro-domain and stabilizing intra-domain contacts. Functionally, SPRING licenses S1P to cleave its cognate substrate, SREBP2. Our findings reveal an activation mechanism for S1P and provide insights into how spatial control of S1P activity underpins cholesterol homeostasis.The authors report the structural basis of site-one protease (S1P) activation by SREBP regulating gene (SPRING). They show that SPRING displaces the inhibitory pro-domain of S1P, enabling S1P to cleave its canonical substrate SREBP2.
Abstract Site-one protease (S1P) conducts the first of two cleavage events in the Golgi to activate Sterol regulatory element binding proteins (SREBPs) and upregulate lipogenic transcription. S1P is also required for a wide array of additional signaling pathways. A zymogen serine protease, S1P matures through autoproteolysis of two pro-domains, with one cleavage event in the endoplasmic reticulum (ER) and the other in the Golgi. We recently identified the SREBP regulating gene, (SPRING), which enhances S1P maturation and is necessary for SREBP signaling. Here, we report the cryo-EM structures of S1P and S1P-SPRING at sub-2.5 Å resolution. SPRING activates S1P by dislodging its inhibitory pro-domain and stabilizing intra-domain contacts. Functionally, SPRING licenses S1P to cleave its cognate substrate, SREBP2. Our findings reveal an activation mechanism for S1P and provide insights into how spatial control of S1P activity underpins cholesterol homeostasis.
Site-one protease (S1P) conducts the first of two cleavage events in the Golgi to activate Sterol regulatory element binding proteins (SREBPs) and upregulate lipogenic transcription. S1P is also required for a wide array of additional signaling pathways. A zymogen serine protease, S1P matures through autoproteolysis of two pro-domains, with one cleavage event in the endoplasmic reticulum (ER) and the other in the Golgi. We recently identified the SREBP regulating gene, (SPRING), which enhances S1P maturation and is necessary for SREBP signaling. Here, we report the cryo-EM structures of S1P and S1P-SPRING at sub-2.5 Å resolution. SPRING activates S1P by dislodging its inhibitory pro-domain and stabilizing intra-domain contacts. Functionally, SPRING licenses S1P to cleave its cognate substrate, SREBP2. Our findings reveal an activation mechanism for S1P and provide insights into how spatial control of S1P activity underpins cholesterol homeostasis. The authors report the structural basis of site-one protease (S1P) activation by SREBP regulating gene (SPRING). They show that SPRING displaces the inhibitory pro-domain of S1P, enabling S1P to cleave its canonical substrate SREBP2.
Site-one protease (S1P) conducts the first of two cleavage events in the Golgi to activate Sterol regulatory element binding proteins (SREBPs) and upregulate lipogenic transcription. S1P is also required for a wide array of additional signaling pathways. A zymogen serine protease, S1P matures through autoproteolysis of two pro-domains, with one cleavage event in the endoplasmic reticulum (ER) and the other in the Golgi. We recently identified the SREBP regulating gene, (SPRING), which enhances S1P maturation and is necessary for SREBP signaling. Here, we report the cryo-EM structures of S1P and S1P-SPRING at sub-2.5 Å resolution. SPRING activates S1P by dislodging its inhibitory pro-domain and stabilizing intra-domain contacts. Functionally, SPRING licenses S1P to cleave its cognate substrate, SREBP2. Our findings reveal an activation mechanism for S1P and provide insights into how spatial control of S1P activity underpins cholesterol homeostasis.Site-one protease (S1P) conducts the first of two cleavage events in the Golgi to activate Sterol regulatory element binding proteins (SREBPs) and upregulate lipogenic transcription. S1P is also required for a wide array of additional signaling pathways. A zymogen serine protease, S1P matures through autoproteolysis of two pro-domains, with one cleavage event in the endoplasmic reticulum (ER) and the other in the Golgi. We recently identified the SREBP regulating gene, (SPRING), which enhances S1P maturation and is necessary for SREBP signaling. Here, we report the cryo-EM structures of S1P and S1P-SPRING at sub-2.5 Å resolution. SPRING activates S1P by dislodging its inhibitory pro-domain and stabilizing intra-domain contacts. Functionally, SPRING licenses S1P to cleave its cognate substrate, SREBP2. Our findings reveal an activation mechanism for S1P and provide insights into how spatial control of S1P activity underpins cholesterol homeostasis.
ArticleNumber 5732
Author Hall, Hailee
Kingma, Jenina
Bajaj, Bilkish
Bawaria, Shrankhla
Dartigue, Vincent
Zelcer, Noam
Kober, Daniel L.
Hendrix, Sebastian
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  surname: Dartigue
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  organization: Department of Biochemistry, The University of Texas Southwestern Medical Center
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  surname: Hall
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  organization: Department of Biochemistry, The University of Texas Southwestern Medical Center
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  surname: Zelcer
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  organization: Department of Medical Biochemistry, Amsterdam UMC, Amsterdam Cardiovascular Sciences and Gastroenterology and Metabolism, University of Amsterdam
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  surname: Kober
  fullname: Kober, Daniel L.
  email: daniel.kober@utsouthwestern.edu
  organization: Department of Biochemistry, The University of Texas Southwestern Medical Center
BackLink https://www.ncbi.nlm.nih.gov/pubmed/38977690$$D View this record in MEDLINE/PubMed
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Snippet Site-one protease (S1P) conducts the first of two cleavage events in the Golgi to activate Sterol regulatory element binding proteins (SREBPs) and upregulate...
Abstract Site-one protease (S1P) conducts the first of two cleavage events in the Golgi to activate Sterol regulatory element binding proteins (SREBPs) and...
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SubjectTerms 101/28
13/106
13/109
631/45/287/1197
631/45/468
631/45/535/1258/1259
82/29
82/83
Animals
Biochemistry
Cholesterol
Cholesterol - metabolism
Cleavage
Cryoelectron Microscopy
Endoplasmic reticulum
Endoplasmic Reticulum - metabolism
Enzymes
Fatty acids
Golgi apparatus
Golgi Apparatus - metabolism
HEK293 Cells
Homeostasis
Humanities and Social Sciences
Humans
Licenses
Metabolism
multidisciplinary
Mutation
Peptides
Proenzymes
Proprotein Convertases - genetics
Proprotein Convertases - metabolism
Protease
Protein Domains
Regulatory sequences
Science
Science (multidisciplinary)
Serine Endopeptidases - chemistry
Serine Endopeptidases - genetics
Serine Endopeptidases - metabolism
Serine proteinase
Signal Transduction
Sterol Regulatory Element Binding Protein 2 - genetics
Sterol Regulatory Element Binding Protein 2 - metabolism
Sterol regulatory element-binding protein
Sterols
Substrates
Transcription factors
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Title SPRING licenses S1P-mediated cleavage of SREBP2 by displacing an inhibitory pro-domain
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