LFA1 Activation: Insights from a Single-Molecule Approach
Integrin LFA1 is a cell adhesion receptor expressed exclusively in leukocytes, and plays crucial roles in lymphocyte trafficking, antigen recognition, and effector functions. Since the discovery that the adhesiveness of LFA1 can be dynamically changed upon stimulation, one challenge has been underst...
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| Format: | Article |
| Language: | English |
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MDPI AG
2022-05-01
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| Series: | Cells |
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| Online Access: | https://www.mdpi.com/2073-4409/11/11/1751 |
| _version_ | 1797493785955926016 |
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| author | Naoyuki Kondo Yoshihiro Ueda Tatsuo Kinashi |
| author_facet | Naoyuki Kondo Yoshihiro Ueda Tatsuo Kinashi |
| author_sort | Naoyuki Kondo |
| collection | DOAJ |
| description | Integrin LFA1 is a cell adhesion receptor expressed exclusively in leukocytes, and plays crucial roles in lymphocyte trafficking, antigen recognition, and effector functions. Since the discovery that the adhesiveness of LFA1 can be dynamically changed upon stimulation, one challenge has been understanding how integrins are regulated by inside-out signaling coupled with macromolecular conformational changes, as well as ligand bindings that transduce signals from the extracellular domain to the cytoplasm in outside-in signaling. The small GTPase Rap1 and integrin adaptor proteins talin1 and kindlin-3 have been recognized as critical molecules for integrin activation. However, their cooperative regulation of integrin adhesiveness in lymphocytes requires further research. Recent advances in single-molecule imaging techniques have revealed dynamic molecular processes in real-time and provided insight into integrin activation in cellular environments. This review summarizes integrin regulation and discusses new findings regarding the bidirectionality of LFA1 activation and signaling processes in lymphocytes. |
| first_indexed | 2024-03-10T01:24:56Z |
| format | Article |
| id | doaj.art-849544f6055b458bb657dca2ffa3eee0 |
| institution | Directory Open Access Journal |
| issn | 2073-4409 |
| language | English |
| last_indexed | 2024-03-10T01:24:56Z |
| publishDate | 2022-05-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Cells |
| spelling | doaj.art-849544f6055b458bb657dca2ffa3eee02023-11-23T13:52:10ZengMDPI AGCells2073-44092022-05-011111175110.3390/cells11111751LFA1 Activation: Insights from a Single-Molecule ApproachNaoyuki Kondo0Yoshihiro Ueda1Tatsuo Kinashi2Department of Molecular Genetics, Institute of Biomedical Science, Kansai Medical University, Osaka 573-1010, JapanDepartment of Molecular Genetics, Institute of Biomedical Science, Kansai Medical University, Osaka 573-1010, JapanDepartment of Molecular Genetics, Institute of Biomedical Science, Kansai Medical University, Osaka 573-1010, JapanIntegrin LFA1 is a cell adhesion receptor expressed exclusively in leukocytes, and plays crucial roles in lymphocyte trafficking, antigen recognition, and effector functions. Since the discovery that the adhesiveness of LFA1 can be dynamically changed upon stimulation, one challenge has been understanding how integrins are regulated by inside-out signaling coupled with macromolecular conformational changes, as well as ligand bindings that transduce signals from the extracellular domain to the cytoplasm in outside-in signaling. The small GTPase Rap1 and integrin adaptor proteins talin1 and kindlin-3 have been recognized as critical molecules for integrin activation. However, their cooperative regulation of integrin adhesiveness in lymphocytes requires further research. Recent advances in single-molecule imaging techniques have revealed dynamic molecular processes in real-time and provided insight into integrin activation in cellular environments. This review summarizes integrin regulation and discusses new findings regarding the bidirectionality of LFA1 activation and signaling processes in lymphocytes.https://www.mdpi.com/2073-4409/11/11/1751LFA1Rap1talinkindlin-3 |
| spellingShingle | Naoyuki Kondo Yoshihiro Ueda Tatsuo Kinashi LFA1 Activation: Insights from a Single-Molecule Approach Cells LFA1 Rap1 talin kindlin-3 |
| title | LFA1 Activation: Insights from a Single-Molecule Approach |
| title_full | LFA1 Activation: Insights from a Single-Molecule Approach |
| title_fullStr | LFA1 Activation: Insights from a Single-Molecule Approach |
| title_full_unstemmed | LFA1 Activation: Insights from a Single-Molecule Approach |
| title_short | LFA1 Activation: Insights from a Single-Molecule Approach |
| title_sort | lfa1 activation insights from a single molecule approach |
| topic | LFA1 Rap1 talin kindlin-3 |
| url | https://www.mdpi.com/2073-4409/11/11/1751 |
| work_keys_str_mv | AT naoyukikondo lfa1activationinsightsfromasinglemoleculeapproach AT yoshihiroueda lfa1activationinsightsfromasinglemoleculeapproach AT tatsuokinashi lfa1activationinsightsfromasinglemoleculeapproach |