Bioinformatics analysis of proteins interacting with different actin isoforms
Actin is one of the most widespread and most conserved proteins. At the same time, six actin isoforms are known, encoded by different genes. These isoforms differ slightly in amino acid sequence and have similar structures, but differ in localization and functioning. During functioning, actin intera...
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| Veröffentlicht in: | Biochemical and biophysical research communications 2025-01, Vol.743, p.151165, Article 151165 |
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| container_title | Biochemical and biophysical research communications |
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| creator | Mokin, Yakov I. Povarova, Olga I. Silonov, Sergey A. Antifeeva, Iuliia A. Uversky, Vladimir N. Turoverov, Konstantin K. Kuznetsova, Irina M. Fonin, Alexander V. |
| description | Actin is one of the most widespread and most conserved proteins. At the same time, six actin isoforms are known, encoded by different genes. These isoforms differ slightly in amino acid sequence and have similar structures, but differ in localization and functioning. During functioning, actin interacts with a large number of proteins, which are combined according to this feature into a pool of so-called actin-binding proteins. The question arises whether and how the proteins interacting with different actin isoforms differ. Since the pool of actin-binding proteins includes hundreds of proteins, it was logical to use bioinformatics analysis to solve the questions. In this work, it is shown that the functionality of the α-, β-, and γ-actin interactomes differ significantly, but their structural characteristics are close.
•Actin is one of the most widespread and most conserved proteins.•In human, six actin isoforms are encoded by different genes.•Isoforms are structurally similar but differ in localization and functioning.•Bioinformatics was used to analyze hundreds of actin-binding proteins.•Functionality of the α-, β-, and γ-actin interactomes differ significantly. |
| doi_str_mv | 10.1016/j.bbrc.2024.151165 |
| format | Article |
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•Actin is one of the most widespread and most conserved proteins.•In human, six actin isoforms are encoded by different genes.•Isoforms are structurally similar but differ in localization and functioning.•Bioinformatics was used to analyze hundreds of actin-binding proteins.•Functionality of the α-, β-, and γ-actin interactomes differ significantly.</description><identifier>ISSN: 0006-291X</identifier><identifier>ISSN: 1090-2104</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/j.bbrc.2024.151165</identifier><identifier>PMID: 39675169</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Actins - chemistry ; Actins - metabolism ; Amino Acid Sequence ; Animals ; Computational Biology - methods ; Humans ; Microfilament Proteins - chemistry ; Microfilament Proteins - genetics ; Microfilament Proteins - metabolism ; Protein Binding ; Protein Isoforms - chemistry ; Protein Isoforms - genetics ; Protein Isoforms - metabolism</subject><ispartof>Biochemical and biophysical research communications, 2025-01, Vol.743, p.151165, Article 151165</ispartof><rights>2024 Elsevier Inc.</rights><rights>Copyright © 2024 Elsevier Inc. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c237t-61161027e5d932fb6bf19d044201e9bf1d5b7220fb92d2bfdefb3e41906c7eb93</cites><orcidid>0000-0002-3336-4834 ; 0000-0001-8714-6659 ; 0000-0002-6977-1896 ; 0009-0006-5930-6647 ; 0000-0003-1568-7493 ; 0000-0002-4037-5857 ; 0000-0003-4469-2531</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0006291X24017017$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/39675169$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Mokin, Yakov I.</creatorcontrib><creatorcontrib>Povarova, Olga I.</creatorcontrib><creatorcontrib>Silonov, Sergey A.</creatorcontrib><creatorcontrib>Antifeeva, Iuliia A.</creatorcontrib><creatorcontrib>Uversky, Vladimir N.</creatorcontrib><creatorcontrib>Turoverov, Konstantin K.</creatorcontrib><creatorcontrib>Kuznetsova, Irina M.</creatorcontrib><creatorcontrib>Fonin, Alexander V.</creatorcontrib><title>Bioinformatics analysis of proteins interacting with different actin isoforms</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>Actin is one of the most widespread and most conserved proteins. At the same time, six actin isoforms are known, encoded by different genes. These isoforms differ slightly in amino acid sequence and have similar structures, but differ in localization and functioning. During functioning, actin interacts with a large number of proteins, which are combined according to this feature into a pool of so-called actin-binding proteins. The question arises whether and how the proteins interacting with different actin isoforms differ. Since the pool of actin-binding proteins includes hundreds of proteins, it was logical to use bioinformatics analysis to solve the questions. In this work, it is shown that the functionality of the α-, β-, and γ-actin interactomes differ significantly, but their structural characteristics are close.
•Actin is one of the most widespread and most conserved proteins.•In human, six actin isoforms are encoded by different genes.•Isoforms are structurally similar but differ in localization and functioning.•Bioinformatics was used to analyze hundreds of actin-binding proteins.•Functionality of the α-, β-, and γ-actin interactomes differ significantly.</description><subject>Actins - chemistry</subject><subject>Actins - metabolism</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Computational Biology - methods</subject><subject>Humans</subject><subject>Microfilament Proteins - chemistry</subject><subject>Microfilament Proteins - genetics</subject><subject>Microfilament Proteins - metabolism</subject><subject>Protein Binding</subject><subject>Protein Isoforms - chemistry</subject><subject>Protein Isoforms - genetics</subject><subject>Protein Isoforms - metabolism</subject><issn>0006-291X</issn><issn>1090-2104</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2025</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kEtPwzAQhC0EouXxBzigHLmk7DqJU0tcAPGSiriAxM2K7TW4apNiu6D-e1JaOHJa7WpmtPMxdoIwQkBxPh1pHcyIAy9HWCGKaocNESTkHKHcZUMAEDmX-DpgBzFOARBLIffZoJCirlDIIXu88p1vXRfmTfImZk3bzFbRx6xz2SJ0iXwbM98mCo1Jvn3Lvnx6z6x3jgK1Kfu5Zj5264h4xPZcM4t0vJ2H7OX25vn6Pp883T1cX05yw4s65aL_FYHXVFlZcKeFdigtlCUHJNkvttI15-C05JZrZ8npgkqUIExNWhaH7GyT27_4saSY1NxHQ7NZ01K3jKroe47LMQL0Ur6RmtDFGMipRfDzJqwUglpjVFO1xqjWGNUGY2863eYv9Zzsn-WXWy-42Aiob_npKahoPLWGrA9kkrKd_y__GyZmhGw</recordid><startdate>202501</startdate><enddate>202501</enddate><creator>Mokin, Yakov I.</creator><creator>Povarova, Olga I.</creator><creator>Silonov, Sergey A.</creator><creator>Antifeeva, Iuliia A.</creator><creator>Uversky, Vladimir N.</creator><creator>Turoverov, Konstantin K.</creator><creator>Kuznetsova, Irina M.</creator><creator>Fonin, Alexander V.</creator><general>Elsevier Inc</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><orcidid>https://orcid.org/0000-0002-3336-4834</orcidid><orcidid>https://orcid.org/0000-0001-8714-6659</orcidid><orcidid>https://orcid.org/0000-0002-6977-1896</orcidid><orcidid>https://orcid.org/0009-0006-5930-6647</orcidid><orcidid>https://orcid.org/0000-0003-1568-7493</orcidid><orcidid>https://orcid.org/0000-0002-4037-5857</orcidid><orcidid>https://orcid.org/0000-0003-4469-2531</orcidid></search><sort><creationdate>202501</creationdate><title>Bioinformatics analysis of proteins interacting with different actin isoforms</title><author>Mokin, Yakov I. ; Povarova, Olga I. ; Silonov, Sergey A. ; Antifeeva, Iuliia A. ; Uversky, Vladimir N. ; Turoverov, Konstantin K. ; Kuznetsova, Irina M. ; Fonin, Alexander V.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c237t-61161027e5d932fb6bf19d044201e9bf1d5b7220fb92d2bfdefb3e41906c7eb93</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2025</creationdate><topic>Actins - chemistry</topic><topic>Actins - metabolism</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Computational Biology - methods</topic><topic>Humans</topic><topic>Microfilament Proteins - chemistry</topic><topic>Microfilament Proteins - genetics</topic><topic>Microfilament Proteins - metabolism</topic><topic>Protein Binding</topic><topic>Protein Isoforms - chemistry</topic><topic>Protein Isoforms - genetics</topic><topic>Protein Isoforms - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Mokin, Yakov I.</creatorcontrib><creatorcontrib>Povarova, Olga I.</creatorcontrib><creatorcontrib>Silonov, Sergey A.</creatorcontrib><creatorcontrib>Antifeeva, Iuliia A.</creatorcontrib><creatorcontrib>Uversky, Vladimir N.</creatorcontrib><creatorcontrib>Turoverov, Konstantin K.</creatorcontrib><creatorcontrib>Kuznetsova, Irina M.</creatorcontrib><creatorcontrib>Fonin, Alexander V.</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>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Mokin, Yakov I.</au><au>Povarova, Olga I.</au><au>Silonov, Sergey A.</au><au>Antifeeva, Iuliia A.</au><au>Uversky, Vladimir N.</au><au>Turoverov, Konstantin K.</au><au>Kuznetsova, Irina M.</au><au>Fonin, Alexander V.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Bioinformatics analysis of proteins interacting with different actin isoforms</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>2025-01</date><risdate>2025</risdate><volume>743</volume><spage>151165</spage><pages>151165-</pages><artnum>151165</artnum><issn>0006-291X</issn><issn>1090-2104</issn><eissn>1090-2104</eissn><abstract>Actin is one of the most widespread and most conserved proteins. At the same time, six actin isoforms are known, encoded by different genes. These isoforms differ slightly in amino acid sequence and have similar structures, but differ in localization and functioning. During functioning, actin interacts with a large number of proteins, which are combined according to this feature into a pool of so-called actin-binding proteins. The question arises whether and how the proteins interacting with different actin isoforms differ. Since the pool of actin-binding proteins includes hundreds of proteins, it was logical to use bioinformatics analysis to solve the questions. In this work, it is shown that the functionality of the α-, β-, and γ-actin interactomes differ significantly, but their structural characteristics are close.
•Actin is one of the most widespread and most conserved proteins.•In human, six actin isoforms are encoded by different genes.•Isoforms are structurally similar but differ in localization and functioning.•Bioinformatics was used to analyze hundreds of actin-binding proteins.•Functionality of the α-, β-, and γ-actin interactomes differ significantly.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>39675169</pmid><doi>10.1016/j.bbrc.2024.151165</doi><orcidid>https://orcid.org/0000-0002-3336-4834</orcidid><orcidid>https://orcid.org/0000-0001-8714-6659</orcidid><orcidid>https://orcid.org/0000-0002-6977-1896</orcidid><orcidid>https://orcid.org/0009-0006-5930-6647</orcidid><orcidid>https://orcid.org/0000-0003-1568-7493</orcidid><orcidid>https://orcid.org/0000-0002-4037-5857</orcidid><orcidid>https://orcid.org/0000-0003-4469-2531</orcidid></addata></record> |
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| subjects | Actins - chemistry Actins - metabolism Amino Acid Sequence Animals Computational Biology - methods Humans Microfilament Proteins - chemistry Microfilament Proteins - genetics Microfilament Proteins - metabolism Protein Binding Protein Isoforms - chemistry Protein Isoforms - genetics Protein Isoforms - metabolism |
| title | Bioinformatics analysis of proteins interacting with different actin isoforms |
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