Characterisation of Kindlin-3 and RACK1 interaction in integrin signaling.
Integrins are cell surface receptors which interact with ECM to induce bidirectional signal to mediate cell spreading. Kindlin-3 is one of the adaptor proteins that will bind and activate integrins and RACK1 is an anchoring protein that is found to be able to interact with β integrin and PH domain o...
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| Format: | Final Year Project |
| Language: | English |
| Published: |
2011
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| Subjects: | |
| Online Access: | http://hdl.handle.net/10356/45616 |
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| Institution: | Nanyang Technological University |
| Language: | English |
| Summary: | Integrins are cell surface receptors which interact with ECM to induce bidirectional signal to mediate cell spreading. Kindlin-3 is one of the adaptor proteins that will bind and activate integrins and RACK1 is an anchoring protein that is found to be able to interact with β integrin and PH domain of other proteins. The main objective of this study was to determine the role of kindlin-3 in integrin outside-in signaling. We showed that kindlin-3 is required for the spreading of cells transfected with constitutively active αLβ2 and αIIbβ3 on their respective ligands. We also demonstrated that kindlin-3 interacts with RACK1 based on pull-down assay using purified recombinant RACK1 and kindlin-3 proteins. We also showed that the PH domain of kindlin-3 interacts with blade 5-7 of RACK1. Future studies will address the interaction of kindlin-3 and RACK1 in integrin outside-in signaling. |
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