Talin2 binds to non-muscle myosin IIa and regulates cell attachment and fibronectin secretion.


Journal

Scientific reports
ISSN: 2045-2322
Titre abrégé: Sci Rep
Pays: England
ID NLM: 101563288

Informations de publication

Date de publication:
30 Aug 2024
Historique:
received: 11 03 2024
accepted: 22 08 2024
medline: 31 8 2024
pubmed: 31 8 2024
entrez: 30 8 2024
Statut: epublish

Résumé

Talin2 is localized to large focal adhesions and is indispensable for traction force generation, invadopodium formation, cell invasion as well as metastasis. Talin2 has a higher affinity toward β-integrin tails than talin1. Moreover, disruption of the talin2-β-integrin interaction inhibits traction force generation, invadopodium formation and cell invasion, indicating that a strong talin2-β-integrin interaction is required for talin2 to fulfill these functions. Nevertheless, the role of talin2 in mediation of these processes remains unknown. Here we show that talin2 binds to the N-terminus of non-muscle myosin IIA (NMIIA) through its F3 subdomain. Moreover, talin2 co-localizes with NMIIA at cell edges as well as at some cytoplasmic spots. Talin2 also co-localizes with cortactin, an invadopodium marker. Furthermore, overexpression of NMIIA promoted the talin2 head binding to the β1-integrin tail, whereas knockdown of NMIIA reduced fibronectin and matrix metalloproteinase secretion as well as inhibited cell attachment on fibronectin-coated substrates. These results suggest that talin2 binds to NMIIA to control the secretion of extracellular matrix proteins and this interaction modulates cell adhesion.

Identifiants

pubmed: 39215026
doi: 10.1038/s41598-024-70866-w
pii: 10.1038/s41598-024-70866-w
pmc: PMC11364542
doi:

Substances chimiques

Talin 0
Fibronectins 0
Nonmuscle Myosin Type IIA EC 3.6.1.-
TLN2 protein, human 0
Integrin beta1 0
Cortactin 0

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

20175

Subventions

Organisme : Polish National Science Centre PRELUDIUM
ID : 2018/31/N/ NZ3/02031
Organisme : Academy of Finland
ID : 331946
Organisme : NIH HHS
ID : GM122994
Pays : United States

Informations de copyright

© 2024. The Author(s).

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Auteurs

Xiaochuan Wang (X)

The Second Hospital of Shandong University, Jinan, 250033, Shandong, China. 2019120219@mail.sdu.edu.cn.

Zbigniew Baster (Z)

Markey Cancer Center, University of Kentucky, Lexington, KY, 40506, USA.
Institute of Physics, Faculty of Physics, Astronomy and Applied Computer Science, Jagiellonian University, 30-348, Kraków, Poland.

Latifeh Azizi (L)

Faculty of Medicine and Health Technology, Tampere University, 33520, Tampere, Finland.
Fimlab Laboratories, Tampere, Finland.

Liqing Li (L)

Markey Cancer Center, University of Kentucky, Lexington, KY, 40506, USA.

Zenon Rajfur (Z)

Institute of Physics, Faculty of Physics, Astronomy and Applied Computer Science, Jagiellonian University, 30-348, Kraków, Poland.
Jagiellonian Center of Biomedical Imaging, Jagiellonian University, 30-348, Kraków, Poland.

Vesa P Hytönen (VP)

Faculty of Medicine and Health Technology, Tampere University, 33520, Tampere, Finland. vesa.hytonen@tuni.fi.
Fimlab Laboratories, Tampere, Finland. vesa.hytonen@tuni.fi.

Cai Huang (C)

Markey Cancer Center, University of Kentucky, Lexington, KY, 40506, USA. caihuang@doerbio.com.
Doer Biologics Inc, 2nd Floor, Building 3, Hexiang Science and Technology Center, Medicine Port Town, Qiantang District, Hangzhou, Zhejiang Province, China. caihuang@doerbio.com.

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