An ULK1/2-PXN mechanotransduction pathway suppresses breast cancer cell migration
The remodeling and stiffening of the extracellular matrix (ECM) is a well-recognized modulator of breast cancer progression. How changes in the mechanical properties of the ECM are converted into biochemical signals that direct tumor cell migration and metastasis remain poorly characterized. Here, w...
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| creator | Liang, Peigang Zhang, Jiaqi Wu, Yuchen Zheng, Shanyuan Xu, Zhaopeng Yang, Shuo Wang, Jinfang Ma, Suibin Xiao, Li Hu, Tianhui Jiang, Wenxue Huang, Chaoqun Xing, Qiong Kundu, Mondira Wang, Bo |
| description | The remodeling and stiffening of the extracellular matrix (ECM) is a well-recognized modulator of breast cancer progression. How changes in the mechanical properties of the ECM are converted into biochemical signals that direct tumor cell migration and metastasis remain poorly characterized. Here, we describe a new role for the autophagy-inducing serine/threonine kinases ULK1 and ULK2 in mechanotransduction. We show that ULK1/2 activity inhibits the assembly of actin stress fibers and focal adhesions (FAs) and as a consequence impedes cell contraction and migration, independent of its role in autophagy. Mechanistically, we identify PXN/paxillin, a key component of the mechanotransducing machinery, as a direct binding partner and substrate of ULK1/2. ULK-mediated phosphorylation of PXN at S32 and S119 weakens homotypic interactions and liquid-liquid phase separation of PXN, impairing FA assembly, which in turn alters the mechanical properties of breast cancer cells and their response to mechanical stimuli. ULK1/2 and the well-characterized PXN regulator, FAK/Src, have opposing functions on mechanotransduction and compete for phosphorylation of adjacent serine and tyrosine residues. Taken together, our study reveals ULK1/2 as important regulator of PXN-dependent mechanotransduction. |
| doi_str_mv | 10.15252/embr.202356850 |
| format | Article |
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How changes in the mechanical properties of the ECM are converted into biochemical signals that direct tumor cell migration and metastasis remain poorly characterized. Here, we describe a new role for the autophagy-inducing serine/threonine kinases ULK1 and ULK2 in mechanotransduction. We show that ULK1/2 activity inhibits the assembly of actin stress fibers and focal adhesions (FAs) and as a consequence impedes cell contraction and migration, independent of its role in autophagy. Mechanistically, we identify PXN/paxillin, a key component of the mechanotransducing machinery, as a direct binding partner and substrate of ULK1/2. ULK-mediated phosphorylation of PXN at S32 and S119 weakens homotypic interactions and liquid-liquid phase separation of PXN, impairing FA assembly, which in turn alters the mechanical properties of breast cancer cells and their response to mechanical stimuli. ULK1/2 and the well-characterized PXN regulator, FAK/Src, have opposing functions on mechanotransduction and compete for phosphorylation of adjacent serine and tyrosine residues. Taken together, our study reveals ULK1/2 as important regulator of PXN-dependent mechanotransduction.</description><identifier>ISSN: 1469-221X</identifier><identifier>ISSN: 1469-3178</identifier><identifier>EISSN: 1469-3178</identifier><identifier>DOI: 10.15252/embr.202356850</identifier><identifier>PMID: 37846507</identifier><language>eng</language><publisher>England: Springer Nature B.V</publisher><subject>Actin ; Assembly ; Autophagy ; Autophagy-Related Protein-1 Homolog - genetics ; Autophagy-Related Protein-1 Homolog - metabolism ; Binding ; Biomaterials ; Biomedical materials ; Breast cancer ; Breast Neoplasms ; Cell adhesion & migration ; Cell migration ; Cell Movement ; Extracellular matrix ; Female ; Fibers ; Humans ; Intracellular Signaling Peptides and Proteins - metabolism ; Kinases ; Liquid phases ; Mechanical properties ; Mechanical stimuli ; Mechanotransduction ; Mechanotransduction, Cellular ; Metastases ; Paxillin ; Paxillin - metabolism ; Phase separation ; Phosphorylation ; Serine ; Serine - metabolism ; Src protein ; Stiffening ; Substrates ; Threonine ; Tyrosine</subject><ispartof>EMBO reports, 2023-11, Vol.24 (11), p.e56850</ispartof><rights>2023 The Authors.</rights><rights>2023 EMBO</rights><rights>2023 The Authors</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c381t-4ffc1ca6122de0bfe4daa8dbaca391efbce1797be277a0b93616a94b357919a63</citedby><cites>FETCH-LOGICAL-c381t-4ffc1ca6122de0bfe4daa8dbaca391efbce1797be277a0b93616a94b357919a63</cites><orcidid>0000-0003-0213-8364 ; 0000-0001-7279-2391 ; 0000-0001-9946-2472 ; 0000-0003-4182-0200 ; 0009-0004-1284-6860 ; 0000-0003-0972-864X</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC10626438/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC10626438/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,27901,27902,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/37846507$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Liang, Peigang</creatorcontrib><creatorcontrib>Zhang, Jiaqi</creatorcontrib><creatorcontrib>Wu, Yuchen</creatorcontrib><creatorcontrib>Zheng, Shanyuan</creatorcontrib><creatorcontrib>Xu, Zhaopeng</creatorcontrib><creatorcontrib>Yang, Shuo</creatorcontrib><creatorcontrib>Wang, Jinfang</creatorcontrib><creatorcontrib>Ma, Suibin</creatorcontrib><creatorcontrib>Xiao, Li</creatorcontrib><creatorcontrib>Hu, Tianhui</creatorcontrib><creatorcontrib>Jiang, Wenxue</creatorcontrib><creatorcontrib>Huang, Chaoqun</creatorcontrib><creatorcontrib>Xing, Qiong</creatorcontrib><creatorcontrib>Kundu, Mondira</creatorcontrib><creatorcontrib>Wang, Bo</creatorcontrib><title>An ULK1/2-PXN mechanotransduction pathway suppresses breast cancer cell migration</title><title>EMBO reports</title><addtitle>EMBO Rep</addtitle><description>The remodeling and stiffening of the extracellular matrix (ECM) is a well-recognized modulator of breast cancer progression. How changes in the mechanical properties of the ECM are converted into biochemical signals that direct tumor cell migration and metastasis remain poorly characterized. Here, we describe a new role for the autophagy-inducing serine/threonine kinases ULK1 and ULK2 in mechanotransduction. We show that ULK1/2 activity inhibits the assembly of actin stress fibers and focal adhesions (FAs) and as a consequence impedes cell contraction and migration, independent of its role in autophagy. Mechanistically, we identify PXN/paxillin, a key component of the mechanotransducing machinery, as a direct binding partner and substrate of ULK1/2. ULK-mediated phosphorylation of PXN at S32 and S119 weakens homotypic interactions and liquid-liquid phase separation of PXN, impairing FA assembly, which in turn alters the mechanical properties of breast cancer cells and their response to mechanical stimuli. ULK1/2 and the well-characterized PXN regulator, FAK/Src, have opposing functions on mechanotransduction and compete for phosphorylation of adjacent serine and tyrosine residues. Taken together, our study reveals ULK1/2 as important regulator of PXN-dependent mechanotransduction.</description><subject>Actin</subject><subject>Assembly</subject><subject>Autophagy</subject><subject>Autophagy-Related Protein-1 Homolog - genetics</subject><subject>Autophagy-Related Protein-1 Homolog - metabolism</subject><subject>Binding</subject><subject>Biomaterials</subject><subject>Biomedical materials</subject><subject>Breast cancer</subject><subject>Breast Neoplasms</subject><subject>Cell adhesion & migration</subject><subject>Cell migration</subject><subject>Cell Movement</subject><subject>Extracellular matrix</subject><subject>Female</subject><subject>Fibers</subject><subject>Humans</subject><subject>Intracellular Signaling Peptides and Proteins - metabolism</subject><subject>Kinases</subject><subject>Liquid phases</subject><subject>Mechanical properties</subject><subject>Mechanical stimuli</subject><subject>Mechanotransduction</subject><subject>Mechanotransduction, Cellular</subject><subject>Metastases</subject><subject>Paxillin</subject><subject>Paxillin - metabolism</subject><subject>Phase separation</subject><subject>Phosphorylation</subject><subject>Serine</subject><subject>Serine - metabolism</subject><subject>Src protein</subject><subject>Stiffening</subject><subject>Substrates</subject><subject>Threonine</subject><subject>Tyrosine</subject><issn>1469-221X</issn><issn>1469-3178</issn><issn>1469-3178</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2023</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpdkc1v1DAQxS0EoqVw5oYiceGSrj1O_HFCVcWXuqJFolJv1tiZdFNtnGAnoP73ZOmyKpxmpPnN03t6jL0W_FTUUMOKep9OgYOslan5E3YsKmVLKbR5ut8BxM0Re5HzHee8tto8Z0dSm0rVXB-zb2exuF5fiBWUVzdfi57CBuMwJYy5mcPUDbEYcdr8wvsiz-OYKGfKhU-EeSoCxkCpCLTdFn13m3DHv2TPWtxmerWfJ-z644fv55_L9eWnL-dn6zJII6ayatsgAioB0BD3LVUNomk8BpRWUOsDCW21J9AaubdSCYW28rLWVlhU8oS9f9AdZ99TEygurrduTF2P6d4N2Ll_L7HbuNvhpxNcgaqkWRTe7RXS8GOmPLm-y7swGGmYswOjDVhpa72gb_9D74Y5xSXfQhkFwCXAQq0eqJCGnBO1BzeCuz99uV1f7tDX8vHmcYgD_7cg-RtXcpLl</recordid><startdate>20231106</startdate><enddate>20231106</enddate><creator>Liang, Peigang</creator><creator>Zhang, Jiaqi</creator><creator>Wu, Yuchen</creator><creator>Zheng, Shanyuan</creator><creator>Xu, Zhaopeng</creator><creator>Yang, Shuo</creator><creator>Wang, Jinfang</creator><creator>Ma, Suibin</creator><creator>Xiao, Li</creator><creator>Hu, Tianhui</creator><creator>Jiang, Wenxue</creator><creator>Huang, Chaoqun</creator><creator>Xing, Qiong</creator><creator>Kundu, Mondira</creator><creator>Wang, Bo</creator><general>Springer Nature B.V</general><general>John Wiley and Sons 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>7QL</scope><scope>7T5</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>K9.</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0003-0213-8364</orcidid><orcidid>https://orcid.org/0000-0001-7279-2391</orcidid><orcidid>https://orcid.org/0000-0001-9946-2472</orcidid><orcidid>https://orcid.org/0000-0003-4182-0200</orcidid><orcidid>https://orcid.org/0009-0004-1284-6860</orcidid><orcidid>https://orcid.org/0000-0003-0972-864X</orcidid></search><sort><creationdate>20231106</creationdate><title>An ULK1/2-PXN mechanotransduction pathway suppresses breast cancer cell migration</title><author>Liang, Peigang ; 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How changes in the mechanical properties of the ECM are converted into biochemical signals that direct tumor cell migration and metastasis remain poorly characterized. Here, we describe a new role for the autophagy-inducing serine/threonine kinases ULK1 and ULK2 in mechanotransduction. We show that ULK1/2 activity inhibits the assembly of actin stress fibers and focal adhesions (FAs) and as a consequence impedes cell contraction and migration, independent of its role in autophagy. Mechanistically, we identify PXN/paxillin, a key component of the mechanotransducing machinery, as a direct binding partner and substrate of ULK1/2. ULK-mediated phosphorylation of PXN at S32 and S119 weakens homotypic interactions and liquid-liquid phase separation of PXN, impairing FA assembly, which in turn alters the mechanical properties of breast cancer cells and their response to mechanical stimuli. ULK1/2 and the well-characterized PXN regulator, FAK/Src, have opposing functions on mechanotransduction and compete for phosphorylation of adjacent serine and tyrosine residues. Taken together, our study reveals ULK1/2 as important regulator of PXN-dependent mechanotransduction.</abstract><cop>England</cop><pub>Springer Nature B.V</pub><pmid>37846507</pmid><doi>10.15252/embr.202356850</doi><orcidid>https://orcid.org/0000-0003-0213-8364</orcidid><orcidid>https://orcid.org/0000-0001-7279-2391</orcidid><orcidid>https://orcid.org/0000-0001-9946-2472</orcidid><orcidid>https://orcid.org/0000-0003-4182-0200</orcidid><orcidid>https://orcid.org/0009-0004-1284-6860</orcidid><orcidid>https://orcid.org/0000-0003-0972-864X</orcidid></addata></record> |
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| subjects | Actin Assembly Autophagy Autophagy-Related Protein-1 Homolog - genetics Autophagy-Related Protein-1 Homolog - metabolism Binding Biomaterials Biomedical materials Breast cancer Breast Neoplasms Cell adhesion & migration Cell migration Cell Movement Extracellular matrix Female Fibers Humans Intracellular Signaling Peptides and Proteins - metabolism Kinases Liquid phases Mechanical properties Mechanical stimuli Mechanotransduction Mechanotransduction, Cellular Metastases Paxillin Paxillin - metabolism Phase separation Phosphorylation Serine Serine - metabolism Src protein Stiffening Substrates Threonine Tyrosine |
| title | An ULK1/2-PXN mechanotransduction pathway suppresses breast cancer cell migration |
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