The actin binding sites of talin have both distinct and complementary roles in cell-ECM adhesion Article Swipe
Darius Camp
,
Bhavya Venkatesh
,
Veronika Solianova
,
Lorena Varela
,
Benjamin T. Goult
,
Guy Tanentzapf
·
YOU?
·
· 2024
· Open Access
·
· DOI: https://doi.org/10.1371/journal.pgen.1011224
YOU?
·
· 2024
· Open Access
·
· DOI: https://doi.org/10.1371/journal.pgen.1011224
Cell adhesion requires linkage of transmembrane receptors to the cytoskeleton through intermediary linker proteins. Integrin-based adhesion to the extracellular matrix (ECM) involves large adhesion complexes that contain multiple cytoskeletal adapters that connect to the actin cytoskeleton. Many of these adapters, including the essential cytoskeletal linker Talin, have been shown to contain multiple actin-binding sites (ABSs) within a single protein. To investigate the possible role of having such a variety of ways of linking integrins to the cytoskeleton, we generated mutations in multiple actin binding sites in Drosophila talin. Using this approach, we have been able to show that different actin-binding sites in talin have both unique and complementary roles in integrin-mediated adhesion. Specifically, mutations in either the C-terminal ABS3 or the centrally located ABS2 result in lethality showing that they have unique and non-redundant function in some contexts. On the other hand, flies simultaneously expressing both the ABS2 and ABS3 mutants exhibit a milder phenotype than either mutant by itself, suggesting overlap in function in other contexts. Detailed phenotypic analysis of ABS mutants elucidated the unique roles of the talin ABSs during embryonic development as well as provided support for the hypothesis that talin acts as a dimer in in vivo contexts. Overall, our work highlights how the ability of adhesion complexes to link to the cytoskeleton in multiple ways provides redundancy, and consequently robustness, but also allows a capacity for functional specialization.
Related Topics
Concepts
Biology
Cell biology
Cytoskeleton
Actin cytoskeleton
Integrin
Cell adhesion
Actin
Actin-binding protein
Genetics
Cell
Metadata
- Type
- article
- Language
- en
- Landing Page
- https://doi.org/10.1371/journal.pgen.1011224
- https://journals.plos.org/plosgenetics/article/file?id=10.1371/journal.pgen.1011224&type=printable
- OA Status
- gold
- Cited By
- 8
- References
- 76
- Related Works
- 10
- OpenAlex ID
- https://openalex.org/W4395447821
All OpenAlex metadata
Raw OpenAlex JSON
- OpenAlex ID
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https://openalex.org/W4395447821Canonical identifier for this work in OpenAlex
- DOI
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https://doi.org/10.1371/journal.pgen.1011224Digital Object Identifier
- Title
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The actin binding sites of talin have both distinct and complementary roles in cell-ECM adhesionWork title
- Type
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articleOpenAlex work type
- Language
-
enPrimary language
- Publication year
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2024Year of publication
- Publication date
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2024-04-25Full publication date if available
- Authors
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Darius Camp, Bhavya Venkatesh, Veronika Solianova, Lorena Varela, Benjamin T. Goult, Guy TanentzapfList of authors in order
- Landing page
-
https://doi.org/10.1371/journal.pgen.1011224Publisher landing page
- PDF URL
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https://journals.plos.org/plosgenetics/article/file?id=10.1371/journal.pgen.1011224&type=printableDirect link to full text PDF
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YesWhether a free full text is available
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goldOpen access status per OpenAlex
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https://journals.plos.org/plosgenetics/article/file?id=10.1371/journal.pgen.1011224&type=printableDirect OA link when available
- Concepts
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Biology, Cell biology, Cytoskeleton, Actin cytoskeleton, Integrin, Cell adhesion, Actin, Actin-binding protein, Genetics, CellTop concepts (fields/topics) attached by OpenAlex
- Cited by
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8Total citation count in OpenAlex
- Citations by year (recent)
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2025: 6, 2024: 2Per-year citation counts (last 5 years)
- References (count)
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76Number of works referenced by this work
- Related works (count)
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10Other works algorithmically related by OpenAlex
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| abstract_inverted_index.Overall, | 202 |
| abstract_inverted_index.adapters | 29 |
| abstract_inverted_index.adhesion | 1, 15, 23, 210 |
| abstract_inverted_index.analysis | 169 |
| abstract_inverted_index.capacity | 229 |
| abstract_inverted_index.function | 134, 163 |
| abstract_inverted_index.involves | 21 |
| abstract_inverted_index.multiple | 27, 51, 81, 218 |
| abstract_inverted_index.possible | 62 |
| abstract_inverted_index.protein. | 58 |
| abstract_inverted_index.provided | 187 |
| abstract_inverted_index.provides | 220 |
| abstract_inverted_index.requires | 2 |
| abstract_inverted_index.adapters, | 39 |
| abstract_inverted_index.adhesion. | 111 |
| abstract_inverted_index.approach, | 90 |
| abstract_inverted_index.centrally | 121 |
| abstract_inverted_index.complexes | 24, 211 |
| abstract_inverted_index.contexts. | 137, 166, 201 |
| abstract_inverted_index.different | 98 |
| abstract_inverted_index.embryonic | 182 |
| abstract_inverted_index.essential | 42 |
| abstract_inverted_index.generated | 78 |
| abstract_inverted_index.including | 40 |
| abstract_inverted_index.integrins | 73 |
| abstract_inverted_index.lethality | 126 |
| abstract_inverted_index.mutations | 79, 113 |
| abstract_inverted_index.phenotype | 154 |
| abstract_inverted_index.proteins. | 13 |
| abstract_inverted_index.receptors | 6 |
| abstract_inverted_index.C-terminal | 117 |
| abstract_inverted_index.Drosophila | 86 |
| abstract_inverted_index.elucidated | 173 |
| abstract_inverted_index.expressing | 144 |
| abstract_inverted_index.functional | 231 |
| abstract_inverted_index.highlights | 205 |
| abstract_inverted_index.hypothesis | 191 |
| abstract_inverted_index.phenotypic | 168 |
| abstract_inverted_index.suggesting | 160 |
| abstract_inverted_index.development | 183 |
| abstract_inverted_index.investigate | 60 |
| abstract_inverted_index.redundancy, | 221 |
| abstract_inverted_index.robustness, | 224 |
| abstract_inverted_index.consequently | 223 |
| abstract_inverted_index.cytoskeletal | 28, 43 |
| abstract_inverted_index.cytoskeleton | 9, 216 |
| abstract_inverted_index.intermediary | 11 |
| abstract_inverted_index.Specifically, | 112 |
| abstract_inverted_index.actin-binding | 52, 99 |
| abstract_inverted_index.complementary | 107 |
| abstract_inverted_index.cytoskeleton, | 76 |
| abstract_inverted_index.cytoskeleton. | 35 |
| abstract_inverted_index.extracellular | 18 |
| abstract_inverted_index.non-redundant | 133 |
| abstract_inverted_index.transmembrane | 5 |
| abstract_inverted_index.Integrin-based | 14 |
| abstract_inverted_index.simultaneously | 143 |
| abstract_inverted_index.specialization. | 232 |
| abstract_inverted_index.integrin-mediated | 110 |
| cited_by_percentile_year.max | 99 |
| cited_by_percentile_year.min | 94 |
| corresponding_author_ids | https://openalex.org/A5054807394, https://openalex.org/A5002928887, https://openalex.org/A5089639893, https://openalex.org/A5061174255, https://openalex.org/A5031601735, https://openalex.org/A5074205395 |
| countries_distinct_count | 2 |
| institutions_distinct_count | 6 |
| corresponding_institution_ids | https://openalex.org/I141945490, https://openalex.org/I20581793 |
| citation_normalized_percentile.value | 0.92443541 |
| citation_normalized_percentile.is_in_top_1_percent | False |
| citation_normalized_percentile.is_in_top_10_percent | True |