The protein kinase Akt acts as a coat adaptor in endocytic recycling
Coat proteins have a central role in vesicular transport by binding to cargoes for their sorting into intracellular pathways. Cargo recognition is mediated by components of the coat complex known as adaptor proteins 1 – 3 . We previously showed that Arf-GAP with coil-coil, ANK repeat and PH domain-c...
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creator | Hsu, Jia-Wei Bai, Ming Li, Kunhua Yang, Jia-Shu Chu, Nam Cole, Philip A. Eck, Michael J. Li, Jian Hsu, Victor W. |
description | Coat proteins have a central role in vesicular transport by binding to cargoes for their sorting into intracellular pathways. Cargo recognition is mediated by components of the coat complex known as adaptor proteins
1
–
3
. We previously showed that Arf-GAP with coil-coil, ANK repeat and PH domain-containing protein 1 (ACAP1) functions as an adaptor for a clathrin coat complex that has a function in endocytic recycling
4
–
6
. Here, we show that the protein kinase Akt acts as a co-adaptor in this complex, and is needed in conjunction with ACAP1 to bind to cargo proteins to promote their recycling. In addition to advancing the understanding of endocytic recycling, we uncover a fundamentally different function in which a kinase acts, as Akt in this case is an effector rather than a regulator in a cellular event.
Hsu et al. find that the protein kinase Akt acts as a co-adaptor in the clathrin coat complex and is needed in conjunction with ACAP1 to bind to cargo proteins to promote their recycling. |
doi_str_mv | 10.1038/s41556-020-0530-z |
format | Article |
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1
–
3
. We previously showed that Arf-GAP with coil-coil, ANK repeat and PH domain-containing protein 1 (ACAP1) functions as an adaptor for a clathrin coat complex that has a function in endocytic recycling
4
–
6
. Here, we show that the protein kinase Akt acts as a co-adaptor in this complex, and is needed in conjunction with ACAP1 to bind to cargo proteins to promote their recycling. In addition to advancing the understanding of endocytic recycling, we uncover a fundamentally different function in which a kinase acts, as Akt in this case is an effector rather than a regulator in a cellular event.
Hsu et al. find that the protein kinase Akt acts as a co-adaptor in the clathrin coat complex and is needed in conjunction with ACAP1 to bind to cargo proteins to promote their recycling.</description><identifier>ISSN: 1465-7392</identifier><identifier>EISSN: 1476-4679</identifier><identifier>DOI: 10.1038/s41556-020-0530-z</identifier><identifier>PMID: 32541877</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>631/80/313/1776 ; 631/80/313/2379 ; Adaptor Proteins, Vesicular Transport - metabolism ; AKT protein ; Biomedical and Life Sciences ; Cancer Research ; Cargo ; Cell Biology ; Cellular control mechanisms ; Clathrin ; Clathrin - metabolism ; Coating ; Coils ; Developmental Biology ; Genetic aspects ; GTPase-Activating Proteins - metabolism ; HEK293 Cells ; HeLa Cells ; Humans ; Integrins - metabolism ; Kinases ; Letter ; Life Sciences ; Observations ; Properties ; Protein Binding ; Protein kinase ; Protein kinases ; Proteins ; Proto-Oncogene Proteins c-akt - metabolism ; Receptors, Transferrin - metabolism ; Stem Cells</subject><ispartof>Nature cell biology, 2020-08, Vol.22 (8), p.927-933</ispartof><rights>The Author(s), under exclusive licence to Springer Nature Limited 2020</rights><rights>COPYRIGHT 2020 Nature Publishing Group</rights><rights>The Author(s), under exclusive licence to Springer Nature Limited 2020.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c637t-db857f5f1493867c517449fb94a35d10d67dde8fcc33f26ebbc4ee5d634217e53</citedby><cites>FETCH-LOGICAL-c637t-db857f5f1493867c517449fb94a35d10d67dde8fcc33f26ebbc4ee5d634217e53</cites><orcidid>0000-0002-9139-4257 ; 0000-0003-4247-9403 ; 0000-0001-9717-5007 ; 0000-0002-6763-4636 ; 0000-0003-3630-0251</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1038/s41556-020-0530-z$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1038/s41556-020-0530-z$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>230,314,776,780,881,27901,27902,41464,42533,51294</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/32541877$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Hsu, Jia-Wei</creatorcontrib><creatorcontrib>Bai, Ming</creatorcontrib><creatorcontrib>Li, Kunhua</creatorcontrib><creatorcontrib>Yang, Jia-Shu</creatorcontrib><creatorcontrib>Chu, Nam</creatorcontrib><creatorcontrib>Cole, Philip A.</creatorcontrib><creatorcontrib>Eck, Michael J.</creatorcontrib><creatorcontrib>Li, Jian</creatorcontrib><creatorcontrib>Hsu, Victor W.</creatorcontrib><title>The protein kinase Akt acts as a coat adaptor in endocytic recycling</title><title>Nature cell biology</title><addtitle>Nat Cell Biol</addtitle><addtitle>Nat Cell Biol</addtitle><description>Coat proteins have a central role in vesicular transport by binding to cargoes for their sorting into intracellular pathways. Cargo recognition is mediated by components of the coat complex known as adaptor proteins
1
–
3
. We previously showed that Arf-GAP with coil-coil, ANK repeat and PH domain-containing protein 1 (ACAP1) functions as an adaptor for a clathrin coat complex that has a function in endocytic recycling
4
–
6
. Here, we show that the protein kinase Akt acts as a co-adaptor in this complex, and is needed in conjunction with ACAP1 to bind to cargo proteins to promote their recycling. In addition to advancing the understanding of endocytic recycling, we uncover a fundamentally different function in which a kinase acts, as Akt in this case is an effector rather than a regulator in a cellular event.
Hsu et al. find that the protein kinase Akt acts as a co-adaptor in the clathrin coat complex and is needed in conjunction with ACAP1 to bind to cargo proteins to promote their recycling.</description><subject>631/80/313/1776</subject><subject>631/80/313/2379</subject><subject>Adaptor Proteins, Vesicular Transport - metabolism</subject><subject>AKT protein</subject><subject>Biomedical and Life Sciences</subject><subject>Cancer Research</subject><subject>Cargo</subject><subject>Cell Biology</subject><subject>Cellular control mechanisms</subject><subject>Clathrin</subject><subject>Clathrin - metabolism</subject><subject>Coating</subject><subject>Coils</subject><subject>Developmental Biology</subject><subject>Genetic aspects</subject><subject>GTPase-Activating Proteins - metabolism</subject><subject>HEK293 Cells</subject><subject>HeLa Cells</subject><subject>Humans</subject><subject>Integrins - metabolism</subject><subject>Kinases</subject><subject>Letter</subject><subject>Life Sciences</subject><subject>Observations</subject><subject>Properties</subject><subject>Protein Binding</subject><subject>Protein kinase</subject><subject>Protein kinases</subject><subject>Proteins</subject><subject>Proto-Oncogene Proteins c-akt - 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metabolism</topic><topic>AKT protein</topic><topic>Biomedical and Life Sciences</topic><topic>Cancer Research</topic><topic>Cargo</topic><topic>Cell Biology</topic><topic>Cellular control mechanisms</topic><topic>Clathrin</topic><topic>Clathrin - metabolism</topic><topic>Coating</topic><topic>Coils</topic><topic>Developmental Biology</topic><topic>Genetic aspects</topic><topic>GTPase-Activating Proteins - metabolism</topic><topic>HEK293 Cells</topic><topic>HeLa Cells</topic><topic>Humans</topic><topic>Integrins - metabolism</topic><topic>Kinases</topic><topic>Letter</topic><topic>Life Sciences</topic><topic>Observations</topic><topic>Properties</topic><topic>Protein Binding</topic><topic>Protein kinase</topic><topic>Protein kinases</topic><topic>Proteins</topic><topic>Proto-Oncogene Proteins c-akt - metabolism</topic><topic>Receptors, Transferrin - metabolism</topic><topic>Stem Cells</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hsu, Jia-Wei</creatorcontrib><creatorcontrib>Bai, Ming</creatorcontrib><creatorcontrib>Li, Kunhua</creatorcontrib><creatorcontrib>Yang, Jia-Shu</creatorcontrib><creatorcontrib>Chu, Nam</creatorcontrib><creatorcontrib>Cole, Philip A.</creatorcontrib><creatorcontrib>Eck, Michael J.</creatorcontrib><creatorcontrib>Li, Jian</creatorcontrib><creatorcontrib>Hsu, Victor W.</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>Immunology Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors 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>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 One Sustainability</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>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>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>Biotechnology and BioEngineering Abstracts</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><collection>PubMed Central (Full Participant titles)</collection><jtitle>Nature cell biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hsu, Jia-Wei</au><au>Bai, Ming</au><au>Li, Kunhua</au><au>Yang, Jia-Shu</au><au>Chu, Nam</au><au>Cole, Philip A.</au><au>Eck, Michael J.</au><au>Li, Jian</au><au>Hsu, Victor W.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The protein kinase Akt acts as a coat adaptor in endocytic recycling</atitle><jtitle>Nature cell biology</jtitle><stitle>Nat Cell Biol</stitle><addtitle>Nat Cell Biol</addtitle><date>2020-08-01</date><risdate>2020</risdate><volume>22</volume><issue>8</issue><spage>927</spage><epage>933</epage><pages>927-933</pages><issn>1465-7392</issn><eissn>1476-4679</eissn><abstract>Coat proteins have a central role in vesicular transport by binding to cargoes for their sorting into intracellular pathways. Cargo recognition is mediated by components of the coat complex known as adaptor proteins
1
–
3
. We previously showed that Arf-GAP with coil-coil, ANK repeat and PH domain-containing protein 1 (ACAP1) functions as an adaptor for a clathrin coat complex that has a function in endocytic recycling
4
–
6
. Here, we show that the protein kinase Akt acts as a co-adaptor in this complex, and is needed in conjunction with ACAP1 to bind to cargo proteins to promote their recycling. In addition to advancing the understanding of endocytic recycling, we uncover a fundamentally different function in which a kinase acts, as Akt in this case is an effector rather than a regulator in a cellular event.
Hsu et al. find that the protein kinase Akt acts as a co-adaptor in the clathrin coat complex and is needed in conjunction with ACAP1 to bind to cargo proteins to promote their recycling.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>32541877</pmid><doi>10.1038/s41556-020-0530-z</doi><tpages>7</tpages><orcidid>https://orcid.org/0000-0002-9139-4257</orcidid><orcidid>https://orcid.org/0000-0003-4247-9403</orcidid><orcidid>https://orcid.org/0000-0001-9717-5007</orcidid><orcidid>https://orcid.org/0000-0002-6763-4636</orcidid><orcidid>https://orcid.org/0000-0003-3630-0251</orcidid><oa>free_for_read</oa></addata></record> |
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subjects | 631/80/313/1776 631/80/313/2379 Adaptor Proteins, Vesicular Transport - metabolism AKT protein Biomedical and Life Sciences Cancer Research Cargo Cell Biology Cellular control mechanisms Clathrin Clathrin - metabolism Coating Coils Developmental Biology Genetic aspects GTPase-Activating Proteins - metabolism HEK293 Cells HeLa Cells Humans Integrins - metabolism Kinases Letter Life Sciences Observations Properties Protein Binding Protein kinase Protein kinases Proteins Proto-Oncogene Proteins c-akt - metabolism Receptors, Transferrin - metabolism Stem Cells |
title | The protein kinase Akt acts as a coat adaptor in endocytic recycling |
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