Diverse functions of myosin VI elucidated by an isoform-specific α-helix domain
- Submitting institution
-
King's College London
- Unit of assessment
- 12 - Engineering
- Output identifier
- 125335399
- Type
- D - Journal article
- DOI
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10.1038/nsmb.3187
- Title of journal
- NATURE STRUCTURAL AND MOLECULAR BIOLOGY
- Article number
- -
- First page
- 300
- Volume
- 23
- Issue
- -
- ISSN
- 1545-9985
- Open access status
- Out of scope for open access requirements
- Month of publication
- March
- Year of publication
- 2016
- URL
-
-
- Supplementary information
-
-
- Request cross-referral to
- 1 - Clinical Medicine
- Output has been delayed by COVID-19
- No
- COVID-19 affected output statement
- -
- Forensic science
- No
- Criminology
- No
- Interdisciplinary
- No
- Number of additional authors
-
12
- Research group(s)
-
-
- Proposed double-weighted
- No
- Reserve for an output with double weighting
- No
- Additional information
- Myosin VI is involved in cell motility. Aberrant myosin VI is one cause of ovarian cancer. This paper found a new structural domain of a myosin VI variant which is responsible of tumor-cell migration. This was enabled by in-silico exon skipping computation, through a novel algorithm for detecting patterns of gene splicing. This research enabled further studies on cell self-degradation (https://doi.org/10.1038/s41467-019-11481-6) and cell membrane transfer (https://doi.org/10.1038/s41467-019-12855-6). This paper highlights the relevance of alternative gene splicing in human diseases, primarily cancer. It provides an important starting point to therapeutically exploit key events in pathological cell migration.
- Author contribution statement
- -
- Non-English
- No
- English abstract
- -