Molecular Insights into the Enigmatic Metabolic Regulator, SnRK1
Sucrose non-fermenting-1 (SNF1)-related kinase 1 (SnRK1) lies at the heart of metabolic homeostasis in plants and is crucial for normal development and response to stress. Evolutionarily related to SNF1 in yeast and AMP-activated kinase (AMPK) in mammals, SnRK1 acts protectively to maintain homeosta...
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Veröffentlicht in: | Trends in plant science 2016-04, Vol.21 (4), p.341-353 |
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description | Sucrose non-fermenting-1 (SNF1)-related kinase 1 (SnRK1) lies at the heart of metabolic homeostasis in plants and is crucial for normal development and response to stress. Evolutionarily related to SNF1 in yeast and AMP-activated kinase (AMPK) in mammals, SnRK1 acts protectively to maintain homeostasis in the face of fluctuations in energy status. Despite a conserved function, the structure and regulation of the plant kinase differ considerably from its relatively well-understood opisthokont orthologues. In this review, we highlight the known plant-specific modes of regulation involving SnRK1 together with new insights based on a 3D molecular model of the kinase. We also summarise how these differences from other orthologues may be specific adaptations to plant metabolism, and offer insights into possible avenues of future inquiry into this enigmatic enzyme.
SnRK1 from plants is a central, enigmatic metabolic regulator that is functionally and evolutionarily related to SNF1 from yeast and AMPK from mammals.
Recent advances have shown that both the subunit structure and regulation of plant SnRK1 differ considerably from those of its better-understood opisthokont orthologues.
SnRK1 acts within complex signalling networks to maintain energy metabolism in plants. The distinct features and regulation, in relation to opisthokonts, likely enable SnRK1 to bring about responses specific to the demands of plant metabolism. |
doi_str_mv | 10.1016/j.tplants.2015.11.001 |
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SnRK1 from plants is a central, enigmatic metabolic regulator that is functionally and evolutionarily related to SNF1 from yeast and AMPK from mammals.
Recent advances have shown that both the subunit structure and regulation of plant SnRK1 differ considerably from those of its better-understood opisthokont orthologues.
SnRK1 acts within complex signalling networks to maintain energy metabolism in plants. The distinct features and regulation, in relation to opisthokonts, likely enable SnRK1 to bring about responses specific to the demands of plant metabolism.</description><identifier>ISSN: 1360-1385</identifier><identifier>EISSN: 1878-4372</identifier><identifier>DOI: 10.1016/j.tplants.2015.11.001</identifier><identifier>PMID: 26642889</identifier><language>eng</language><publisher>England: Elsevier Ltd</publisher><subject>Adaptation, Physiological ; AMP-activated protein kinase (AMPK) ; Arabidopsis - enzymology ; Arabidopsis - genetics ; Arabidopsis - physiology ; Arabidopsis Proteins - chemistry ; Arabidopsis Proteins - genetics ; Arabidopsis Proteins - metabolism ; Gene Expression Regulation, Plant ; Homeostasis ; Models, Molecular ; phosphorylation ; plant metabolic control ; Plants - enzymology ; Plants - genetics ; Protein-Serine-Threonine Kinases - chemistry ; Protein-Serine-Threonine Kinases - genetics ; Protein-Serine-Threonine Kinases - metabolism ; SNF1-related kinase 1 (SnRK1) ; Species Specificity ; Sucrose - metabolism ; sucrose non-fermenting 1 (SNF1) ; trehalose-6-phosphate (T6P)</subject><ispartof>Trends in plant science, 2016-04, Vol.21 (4), p.341-353</ispartof><rights>2015 Elsevier Ltd</rights><rights>Copyright © 2015 Elsevier Ltd. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c365t-c453dc19f5bd16adb30f7de497e27775eb4118ea262e27e4eb6e7531d84348af3</citedby><cites>FETCH-LOGICAL-c365t-c453dc19f5bd16adb30f7de497e27775eb4118ea262e27e4eb6e7531d84348af3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S1360138515002812$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/26642889$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Emanuelle, Shane</creatorcontrib><creatorcontrib>Doblin, Monika S.</creatorcontrib><creatorcontrib>Stapleton, David I.</creatorcontrib><creatorcontrib>Bacic, Antony</creatorcontrib><creatorcontrib>Gooley, Paul R.</creatorcontrib><title>Molecular Insights into the Enigmatic Metabolic Regulator, SnRK1</title><title>Trends in plant science</title><addtitle>Trends Plant Sci</addtitle><description>Sucrose non-fermenting-1 (SNF1)-related kinase 1 (SnRK1) lies at the heart of metabolic homeostasis in plants and is crucial for normal development and response to stress. Evolutionarily related to SNF1 in yeast and AMP-activated kinase (AMPK) in mammals, SnRK1 acts protectively to maintain homeostasis in the face of fluctuations in energy status. Despite a conserved function, the structure and regulation of the plant kinase differ considerably from its relatively well-understood opisthokont orthologues. In this review, we highlight the known plant-specific modes of regulation involving SnRK1 together with new insights based on a 3D molecular model of the kinase. We also summarise how these differences from other orthologues may be specific adaptations to plant metabolism, and offer insights into possible avenues of future inquiry into this enigmatic enzyme.
SnRK1 from plants is a central, enigmatic metabolic regulator that is functionally and evolutionarily related to SNF1 from yeast and AMPK from mammals.
Recent advances have shown that both the subunit structure and regulation of plant SnRK1 differ considerably from those of its better-understood opisthokont orthologues.
SnRK1 acts within complex signalling networks to maintain energy metabolism in plants. The distinct features and regulation, in relation to opisthokonts, likely enable SnRK1 to bring about responses specific to the demands of plant metabolism.</description><subject>Adaptation, Physiological</subject><subject>AMP-activated protein kinase (AMPK)</subject><subject>Arabidopsis - enzymology</subject><subject>Arabidopsis - genetics</subject><subject>Arabidopsis - physiology</subject><subject>Arabidopsis Proteins - chemistry</subject><subject>Arabidopsis Proteins - genetics</subject><subject>Arabidopsis Proteins - metabolism</subject><subject>Gene Expression Regulation, Plant</subject><subject>Homeostasis</subject><subject>Models, Molecular</subject><subject>phosphorylation</subject><subject>plant metabolic control</subject><subject>Plants - enzymology</subject><subject>Plants - genetics</subject><subject>Protein-Serine-Threonine Kinases - chemistry</subject><subject>Protein-Serine-Threonine Kinases - genetics</subject><subject>Protein-Serine-Threonine Kinases - metabolism</subject><subject>SNF1-related kinase 1 (SnRK1)</subject><subject>Species Specificity</subject><subject>Sucrose - metabolism</subject><subject>sucrose non-fermenting 1 (SNF1)</subject><subject>trehalose-6-phosphate (T6P)</subject><issn>1360-1385</issn><issn>1878-4372</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkMtOwzAQRS0E4v0JoCxZkOCJHdtdAap4iVZIPNaW40yKqzQptovE32PUwpbVXI3OzGgOISdAC6AgLuZFXHamj6EoKVQFQEEpbJF9UFLlnMlyO2UmaA5MVXvkIIQ5pVSCErtkrxSCl0qN9snVdOjQrjrjs4c-uNl7DJnr45DFd8xuejdbmOhsNsVo6qFL6RlniY6DP89e-udHOCI7rekCHm_qIXm7vXkd3-eTp7uH8fUkt0xUMbe8Yo2FUVvVDQjT1Iy2skE-klhKKSusOYBCU4oyNZBjLVBWDBrFGVemZYfkbL136YePFYaoFy5Y7JIDHFZBg5SKU-BSJbRao9YPIXhs9dK7hfFfGqj-kafneiNP_8jTADrJS3OnmxOreoHN39SvrQRcrgFMj3469DpYh73Fxnm0UTeD--fENw4NgmA</recordid><startdate>201604</startdate><enddate>201604</enddate><creator>Emanuelle, Shane</creator><creator>Doblin, Monika S.</creator><creator>Stapleton, David I.</creator><creator>Bacic, Antony</creator><creator>Gooley, Paul R.</creator><general>Elsevier Ltd</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>201604</creationdate><title>Molecular Insights into the Enigmatic Metabolic Regulator, SnRK1</title><author>Emanuelle, Shane ; Doblin, Monika S. ; Stapleton, David I. ; Bacic, Antony ; Gooley, Paul R.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c365t-c453dc19f5bd16adb30f7de497e27775eb4118ea262e27e4eb6e7531d84348af3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2016</creationdate><topic>Adaptation, Physiological</topic><topic>AMP-activated protein kinase (AMPK)</topic><topic>Arabidopsis - enzymology</topic><topic>Arabidopsis - genetics</topic><topic>Arabidopsis - physiology</topic><topic>Arabidopsis Proteins - chemistry</topic><topic>Arabidopsis Proteins - genetics</topic><topic>Arabidopsis Proteins - metabolism</topic><topic>Gene Expression Regulation, Plant</topic><topic>Homeostasis</topic><topic>Models, Molecular</topic><topic>phosphorylation</topic><topic>plant metabolic control</topic><topic>Plants - enzymology</topic><topic>Plants - genetics</topic><topic>Protein-Serine-Threonine Kinases - chemistry</topic><topic>Protein-Serine-Threonine Kinases - genetics</topic><topic>Protein-Serine-Threonine Kinases - metabolism</topic><topic>SNF1-related kinase 1 (SnRK1)</topic><topic>Species Specificity</topic><topic>Sucrose - metabolism</topic><topic>sucrose non-fermenting 1 (SNF1)</topic><topic>trehalose-6-phosphate (T6P)</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Emanuelle, Shane</creatorcontrib><creatorcontrib>Doblin, Monika S.</creatorcontrib><creatorcontrib>Stapleton, David I.</creatorcontrib><creatorcontrib>Bacic, Antony</creatorcontrib><creatorcontrib>Gooley, Paul R.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Trends in plant science</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Emanuelle, Shane</au><au>Doblin, Monika S.</au><au>Stapleton, David I.</au><au>Bacic, Antony</au><au>Gooley, Paul R.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Molecular Insights into the Enigmatic Metabolic Regulator, SnRK1</atitle><jtitle>Trends in plant science</jtitle><addtitle>Trends Plant Sci</addtitle><date>2016-04</date><risdate>2016</risdate><volume>21</volume><issue>4</issue><spage>341</spage><epage>353</epage><pages>341-353</pages><issn>1360-1385</issn><eissn>1878-4372</eissn><abstract>Sucrose non-fermenting-1 (SNF1)-related kinase 1 (SnRK1) lies at the heart of metabolic homeostasis in plants and is crucial for normal development and response to stress. Evolutionarily related to SNF1 in yeast and AMP-activated kinase (AMPK) in mammals, SnRK1 acts protectively to maintain homeostasis in the face of fluctuations in energy status. Despite a conserved function, the structure and regulation of the plant kinase differ considerably from its relatively well-understood opisthokont orthologues. In this review, we highlight the known plant-specific modes of regulation involving SnRK1 together with new insights based on a 3D molecular model of the kinase. We also summarise how these differences from other orthologues may be specific adaptations to plant metabolism, and offer insights into possible avenues of future inquiry into this enigmatic enzyme.
SnRK1 from plants is a central, enigmatic metabolic regulator that is functionally and evolutionarily related to SNF1 from yeast and AMPK from mammals.
Recent advances have shown that both the subunit structure and regulation of plant SnRK1 differ considerably from those of its better-understood opisthokont orthologues.
SnRK1 acts within complex signalling networks to maintain energy metabolism in plants. The distinct features and regulation, in relation to opisthokonts, likely enable SnRK1 to bring about responses specific to the demands of plant metabolism.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>26642889</pmid><doi>10.1016/j.tplants.2015.11.001</doi><tpages>13</tpages></addata></record> |
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subjects | Adaptation, Physiological AMP-activated protein kinase (AMPK) Arabidopsis - enzymology Arabidopsis - genetics Arabidopsis - physiology Arabidopsis Proteins - chemistry Arabidopsis Proteins - genetics Arabidopsis Proteins - metabolism Gene Expression Regulation, Plant Homeostasis Models, Molecular phosphorylation plant metabolic control Plants - enzymology Plants - genetics Protein-Serine-Threonine Kinases - chemistry Protein-Serine-Threonine Kinases - genetics Protein-Serine-Threonine Kinases - metabolism SNF1-related kinase 1 (SnRK1) Species Specificity Sucrose - metabolism sucrose non-fermenting 1 (SNF1) trehalose-6-phosphate (T6P) |
title | Molecular Insights into the Enigmatic Metabolic Regulator, SnRK1 |
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