Investigation of the adaptor protein PLIC-2 in multiple pathways
PLIC, Protein Linking IAP (CD47) to Cytoskeleton, have long since been implicated in connecting the extracellular membrane to the intracellular cell cytoskeleton. This phenomenon is supposedly achieved by bridging a receptor protein CD47 to vimentin, an intermediate filament, which in turn regulates...
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| Format: | Article |
| Language: | English |
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Elsevier
2017-03-01
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| Series: | Biochemistry and Biophysics Reports |
| Subjects: | |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S2405580816301856 |
| _version_ | 1811220841213460480 |
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| author | Khiem Nguyen Robbins Puthenveetil Olga Vinogradova |
| author_facet | Khiem Nguyen Robbins Puthenveetil Olga Vinogradova |
| author_sort | Khiem Nguyen |
| collection | DOAJ |
| description | PLIC, Protein Linking IAP (CD47) to Cytoskeleton, have long since been implicated in connecting the extracellular membrane to the intracellular cell cytoskeleton. This phenomenon is supposedly achieved by bridging a receptor protein CD47 to vimentin, an intermediate filament, which in turn regulates integrin dependent cell spreading. Since the discovery of these proteins, the molecular details of the above-mentioned interactions and the underlying complexes are yet to be characterized. Several independent studies have together emphasized PLIC/Ubiquilin’s role in the proteasomal degradation pathway. This seems to be in contrast to the purported initial discovery of PLIC as a cytoskeletal adaptor protein. In an effort to reconcile the different roles associated with the ubiquitous PLIC proteins, we tested the involvement of PLIC-2 both in the proteasomal degradation pathway and as a protein linking the cell cytoskeleton to the cytoplasmic tail of CD47. This was achieved thorough an in vitro investigation of their binding interface using a combination of biophysical techniques. Our results show that the two terminal domains of PLIC-2 interact weakly with each other, while the C-terminal UBA domain interacts strongly with ubiquitin. Interestingly, no perceptible interaction was observed for PLIC-2 with the cytoplasmic tail of CD47 questioning its role as a “PLIC” protein linking the cell membrane to the cytoskeleton. |
| first_indexed | 2024-04-12T07:48:42Z |
| format | Article |
| id | doaj.art-1c2b8779319b4d9f9e9691a7a55ffaa8 |
| institution | Directory Open Access Journal |
| issn | 2405-5808 |
| language | English |
| last_indexed | 2024-04-12T07:48:42Z |
| publishDate | 2017-03-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Biochemistry and Biophysics Reports |
| spelling | doaj.art-1c2b8779319b4d9f9e9691a7a55ffaa82022-12-22T03:41:38ZengElsevierBiochemistry and Biophysics Reports2405-58082017-03-019C34134810.1016/j.bbrep.2017.01.013Investigation of the adaptor protein PLIC-2 in multiple pathwaysKhiem Nguyen0Robbins Puthenveetil1Olga Vinogradova2Department of Pharmaceutical Sciences, School of Pharmacy, University of Connecticut at Storrs, Storrs, CT 06269, USADepartment of Molecular and Cell Biology, CLAS, University of Connecticut at Storrs, Storrs, CT 06269, USADepartment of Pharmaceutical Sciences, School of Pharmacy, University of Connecticut at Storrs, Storrs, CT 06269, USAPLIC, Protein Linking IAP (CD47) to Cytoskeleton, have long since been implicated in connecting the extracellular membrane to the intracellular cell cytoskeleton. This phenomenon is supposedly achieved by bridging a receptor protein CD47 to vimentin, an intermediate filament, which in turn regulates integrin dependent cell spreading. Since the discovery of these proteins, the molecular details of the above-mentioned interactions and the underlying complexes are yet to be characterized. Several independent studies have together emphasized PLIC/Ubiquilin’s role in the proteasomal degradation pathway. This seems to be in contrast to the purported initial discovery of PLIC as a cytoskeletal adaptor protein. In an effort to reconcile the different roles associated with the ubiquitous PLIC proteins, we tested the involvement of PLIC-2 both in the proteasomal degradation pathway and as a protein linking the cell cytoskeleton to the cytoplasmic tail of CD47. This was achieved thorough an in vitro investigation of their binding interface using a combination of biophysical techniques. Our results show that the two terminal domains of PLIC-2 interact weakly with each other, while the C-terminal UBA domain interacts strongly with ubiquitin. Interestingly, no perceptible interaction was observed for PLIC-2 with the cytoplasmic tail of CD47 questioning its role as a “PLIC” protein linking the cell membrane to the cytoskeleton.http://www.sciencedirect.com/science/article/pii/S2405580816301856CD47PLICUbiquilinUBAUBLNanodiscProteasomal degradationVimentinTransmembraneCytoplasmic tailMembrane proteinsNMRITC |
| spellingShingle | Khiem Nguyen Robbins Puthenveetil Olga Vinogradova Investigation of the adaptor protein PLIC-2 in multiple pathways Biochemistry and Biophysics Reports CD47 PLIC Ubiquilin UBA UBL Nanodisc Proteasomal degradation Vimentin Transmembrane Cytoplasmic tail Membrane proteins NMR ITC |
| title | Investigation of the adaptor protein PLIC-2 in multiple pathways |
| title_full | Investigation of the adaptor protein PLIC-2 in multiple pathways |
| title_fullStr | Investigation of the adaptor protein PLIC-2 in multiple pathways |
| title_full_unstemmed | Investigation of the adaptor protein PLIC-2 in multiple pathways |
| title_short | Investigation of the adaptor protein PLIC-2 in multiple pathways |
| title_sort | investigation of the adaptor protein plic 2 in multiple pathways |
| topic | CD47 PLIC Ubiquilin UBA UBL Nanodisc Proteasomal degradation Vimentin Transmembrane Cytoplasmic tail Membrane proteins NMR ITC |
| url | http://www.sciencedirect.com/science/article/pii/S2405580816301856 |
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