Function and regulation of Rnd proteins
Key Points The three Rnd proteins appeared late in evolution (in vertebrates) and are Rho-family proteins with unusual biochemical properties. They do not cycle between GDP (inactive) and GTP (active) states, but are constitutively active (GTP bound). Because Rnd proteins are constitutively active a...
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description | Key Points
The three Rnd proteins appeared late in evolution (in vertebrates) and are Rho-family proteins with unusual biochemical properties. They do not cycle between GDP (inactive) and GTP (active) states, but are constitutively active (GTP bound).
Because Rnd proteins are constitutively active and do not cycle, they are regulated by other mechanisms, including expression levels, localization, phosphorylation and degradation.
Rnd proteins have effects antagonistic to Rho, and they inhibit the formation of contractile acto-myosin cables (stress fibres). Rnd proteins are expressed in neurons where they participate in the extension of growth cones.
Rnd proteins are involved in axon guidance and interact with plexins (the semaphorin receptors) to modulate downstream pathways. Rnd proteins are also involved in fibroblast-growth-factor-receptor-1 signalling.
Rnd3 overexpression blocks cell-cycle progression, and Rnd3 protein expression is frequently decreased in prostate and breast cancer. However, increased expression of Rnd3 has also been observed in cancers with a constitutively active Ras–Raf pathway. Additional studies are required to understand the basis for these apparent discrepancies.
Further studies in animal models are needed to investigate the roles of Rnd proteins in brain development, and a more precise understanding of the functions of Rnd partners is required. A role in axonal regeneration of injured nerve cells is another exciting possibility.
The Rnd proteins, which form a distinct sub-group of the Rho family of small GTP-binding proteins, have been shown to regulate the organization of the actin cytoskeleton in several tissues. In the brain, they participate in neurite extension, whereas in smooth muscle, they modulate contractility. Recent evidence has shown that Rnd3 (RhoE) is also involved in the regulation of cell-cycle progression and transformation, indicating that these proteins might have other, as yet unexplored roles. |
doi_str_mv | 10.1038/nrm1788 |
format | Article |
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The three Rnd proteins appeared late in evolution (in vertebrates) and are Rho-family proteins with unusual biochemical properties. They do not cycle between GDP (inactive) and GTP (active) states, but are constitutively active (GTP bound).
Because Rnd proteins are constitutively active and do not cycle, they are regulated by other mechanisms, including expression levels, localization, phosphorylation and degradation.
Rnd proteins have effects antagonistic to Rho, and they inhibit the formation of contractile acto-myosin cables (stress fibres). Rnd proteins are expressed in neurons where they participate in the extension of growth cones.
Rnd proteins are involved in axon guidance and interact with plexins (the semaphorin receptors) to modulate downstream pathways. Rnd proteins are also involved in fibroblast-growth-factor-receptor-1 signalling.
Rnd3 overexpression blocks cell-cycle progression, and Rnd3 protein expression is frequently decreased in prostate and breast cancer. However, increased expression of Rnd3 has also been observed in cancers with a constitutively active Ras–Raf pathway. Additional studies are required to understand the basis for these apparent discrepancies.
Further studies in animal models are needed to investigate the roles of Rnd proteins in brain development, and a more precise understanding of the functions of Rnd partners is required. A role in axonal regeneration of injured nerve cells is another exciting possibility.
The Rnd proteins, which form a distinct sub-group of the Rho family of small GTP-binding proteins, have been shown to regulate the organization of the actin cytoskeleton in several tissues. In the brain, they participate in neurite extension, whereas in smooth muscle, they modulate contractility. Recent evidence has shown that Rnd3 (RhoE) is also involved in the regulation of cell-cycle progression and transformation, indicating that these proteins might have other, as yet unexplored roles.</description><identifier>ISSN: 1471-0072</identifier><identifier>EISSN: 1471-0080</identifier><identifier>DOI: 10.1038/nrm1788</identifier><identifier>PMID: 16493413</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>Actins - metabolism ; Animals ; Axons - physiology ; Axons - ultrastructure ; Biochemistry ; Biomedical and Life Sciences ; Cancer Research ; Cell Biology ; Cell Cycle ; Cytoskeleton ; Cytoskeleton - metabolism ; Developmental Biology ; Humans ; Life Sciences ; Localization ; Nematodes ; Neurites - physiology ; Neurites - ultrastructure ; Proteins ; review-article ; rho GTP-Binding Proteins - metabolism ; Stem Cells</subject><ispartof>Nature reviews. Molecular cell biology, 2006-01, Vol.7 (1), p.54-62</ispartof><rights>Springer Nature Limited 2006</rights><rights>COPYRIGHT 2006 Nature Publishing Group</rights><rights>Copyright Nature Publishing Group Jan 2006</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c493t-c65251d90e4ba7f5761ec3c5ab5e9d85c879b1ff4b3c967ffb36457b95feb93</citedby><cites>FETCH-LOGICAL-c493t-c65251d90e4ba7f5761ec3c5ab5e9d85c879b1ff4b3c967ffb36457b95feb93</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,2727,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16493413$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Chardin, Pierre</creatorcontrib><title>Function and regulation of Rnd proteins</title><title>Nature reviews. Molecular cell biology</title><addtitle>Nat Rev Mol Cell Biol</addtitle><addtitle>Nat Rev Mol Cell Biol</addtitle><description>Key Points
The three Rnd proteins appeared late in evolution (in vertebrates) and are Rho-family proteins with unusual biochemical properties. They do not cycle between GDP (inactive) and GTP (active) states, but are constitutively active (GTP bound).
Because Rnd proteins are constitutively active and do not cycle, they are regulated by other mechanisms, including expression levels, localization, phosphorylation and degradation.
Rnd proteins have effects antagonistic to Rho, and they inhibit the formation of contractile acto-myosin cables (stress fibres). Rnd proteins are expressed in neurons where they participate in the extension of growth cones.
Rnd proteins are involved in axon guidance and interact with plexins (the semaphorin receptors) to modulate downstream pathways. Rnd proteins are also involved in fibroblast-growth-factor-receptor-1 signalling.
Rnd3 overexpression blocks cell-cycle progression, and Rnd3 protein expression is frequently decreased in prostate and breast cancer. However, increased expression of Rnd3 has also been observed in cancers with a constitutively active Ras–Raf pathway. Additional studies are required to understand the basis for these apparent discrepancies.
Further studies in animal models are needed to investigate the roles of Rnd proteins in brain development, and a more precise understanding of the functions of Rnd partners is required. A role in axonal regeneration of injured nerve cells is another exciting possibility.
The Rnd proteins, which form a distinct sub-group of the Rho family of small GTP-binding proteins, have been shown to regulate the organization of the actin cytoskeleton in several tissues. In the brain, they participate in neurite extension, whereas in smooth muscle, they modulate contractility. Recent evidence has shown that Rnd3 (RhoE) is also involved in the regulation of cell-cycle progression and transformation, indicating that these proteins might have other, as yet unexplored roles.</description><subject>Actins - metabolism</subject><subject>Animals</subject><subject>Axons - physiology</subject><subject>Axons - ultrastructure</subject><subject>Biochemistry</subject><subject>Biomedical and Life Sciences</subject><subject>Cancer Research</subject><subject>Cell Biology</subject><subject>Cell Cycle</subject><subject>Cytoskeleton</subject><subject>Cytoskeleton - metabolism</subject><subject>Developmental Biology</subject><subject>Humans</subject><subject>Life Sciences</subject><subject>Localization</subject><subject>Nematodes</subject><subject>Neurites - physiology</subject><subject>Neurites - ultrastructure</subject><subject>Proteins</subject><subject>review-article</subject><subject>rho GTP-Binding Proteins - metabolism</subject><subject>Stem Cells</subject><issn>1471-0072</issn><issn>1471-0080</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNqF0V1LHDEUBuBQWqpV8Re0LBZqvVjNmXxfitRWEArqfchkTpaRmYxNZkD_fbOdrbJtoeQiX0_ecDiEHAI9Bcr0WUw9KK1fkV3gCpaUavr6ea2qHfIu53tKQYISb8kOSG4YB7ZLji-n6Md2iAsXm0XC1dS5X9shLG7KyUMaRmxj3idvgusyHmzmPXJ7-eXu4tvy-vvXq4vz66UviePSS1EJaAxFXjsVhJKAnnnhaoGm0cJrZWoIgdfMG6lCqJnkQtVGBKwN2yOf5tTy7Y8J82j7NnvsOhdxmLKVSmoBUv0XgqKKGraGR3_A-2FKsZRgq4pLqSXnBX2c0cp1aNsYhjE5v06056C1gYqBKOr0H6qMBvvWDxFDW863HpxsPShmxMdx5aac7dXtzbY9nq1PQ84Jg31Ibe_SkwVq1y22mxYX-WFT0VT32Ly4TU8L-DyDXK7iCtNLyX9nvZ9pdOOU8Dnr9_1PI-K0wA</recordid><startdate>200601</startdate><enddate>200601</enddate><creator>Chardin, Pierre</creator><general>Nature Publishing Group UK</general><general>Nature Publishing Group</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>ISR</scope><scope>3V.</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7RV</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>BKSAR</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB0</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>NAPCQ</scope><scope>P64</scope><scope>PCBAR</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>200601</creationdate><title>Function and regulation of Rnd proteins</title><author>Chardin, Pierre</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c493t-c65251d90e4ba7f5761ec3c5ab5e9d85c879b1ff4b3c967ffb36457b95feb93</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Actins - metabolism</topic><topic>Animals</topic><topic>Axons - physiology</topic><topic>Axons - ultrastructure</topic><topic>Biochemistry</topic><topic>Biomedical and Life Sciences</topic><topic>Cancer Research</topic><topic>Cell Biology</topic><topic>Cell Cycle</topic><topic>Cytoskeleton</topic><topic>Cytoskeleton - metabolism</topic><topic>Developmental Biology</topic><topic>Humans</topic><topic>Life Sciences</topic><topic>Localization</topic><topic>Nematodes</topic><topic>Neurites - physiology</topic><topic>Neurites - ultrastructure</topic><topic>Proteins</topic><topic>review-article</topic><topic>rho GTP-Binding Proteins - metabolism</topic><topic>Stem Cells</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Chardin, Pierre</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Gale In Context: Science</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Nursing & Allied Health Database</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Public Health Database</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>Earth, Atmospheric & Aquatic Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Nursing & Allied Health Database (Alumni Edition)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Nursing & Allied Health Premium</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Earth, Atmospheric & Aquatic Science Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Nature reviews. Molecular cell biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Chardin, Pierre</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Function and regulation of Rnd proteins</atitle><jtitle>Nature reviews. Molecular cell biology</jtitle><stitle>Nat Rev Mol Cell Biol</stitle><addtitle>Nat Rev Mol Cell Biol</addtitle><date>2006-01</date><risdate>2006</risdate><volume>7</volume><issue>1</issue><spage>54</spage><epage>62</epage><pages>54-62</pages><issn>1471-0072</issn><eissn>1471-0080</eissn><abstract>Key Points
The three Rnd proteins appeared late in evolution (in vertebrates) and are Rho-family proteins with unusual biochemical properties. They do not cycle between GDP (inactive) and GTP (active) states, but are constitutively active (GTP bound).
Because Rnd proteins are constitutively active and do not cycle, they are regulated by other mechanisms, including expression levels, localization, phosphorylation and degradation.
Rnd proteins have effects antagonistic to Rho, and they inhibit the formation of contractile acto-myosin cables (stress fibres). Rnd proteins are expressed in neurons where they participate in the extension of growth cones.
Rnd proteins are involved in axon guidance and interact with plexins (the semaphorin receptors) to modulate downstream pathways. Rnd proteins are also involved in fibroblast-growth-factor-receptor-1 signalling.
Rnd3 overexpression blocks cell-cycle progression, and Rnd3 protein expression is frequently decreased in prostate and breast cancer. However, increased expression of Rnd3 has also been observed in cancers with a constitutively active Ras–Raf pathway. Additional studies are required to understand the basis for these apparent discrepancies.
Further studies in animal models are needed to investigate the roles of Rnd proteins in brain development, and a more precise understanding of the functions of Rnd partners is required. A role in axonal regeneration of injured nerve cells is another exciting possibility.
The Rnd proteins, which form a distinct sub-group of the Rho family of small GTP-binding proteins, have been shown to regulate the organization of the actin cytoskeleton in several tissues. In the brain, they participate in neurite extension, whereas in smooth muscle, they modulate contractility. Recent evidence has shown that Rnd3 (RhoE) is also involved in the regulation of cell-cycle progression and transformation, indicating that these proteins might have other, as yet unexplored roles.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>16493413</pmid><doi>10.1038/nrm1788</doi><tpages>9</tpages></addata></record> |
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subjects | Actins - metabolism Animals Axons - physiology Axons - ultrastructure Biochemistry Biomedical and Life Sciences Cancer Research Cell Biology Cell Cycle Cytoskeleton Cytoskeleton - metabolism Developmental Biology Humans Life Sciences Localization Nematodes Neurites - physiology Neurites - ultrastructure Proteins review-article rho GTP-Binding Proteins - metabolism Stem Cells |
title | Function and regulation of Rnd proteins |
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