ArticleBMC cell biology2014
Tissue specific expression of myosin IC isoforms.
Article in BMC cell biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 21 citations in OpenAlex.
- Myosin Class I Genes Follow a Cell Type-Specific Transcription Pattern in Human Haematopoietic Cell Lines.International journal of molecular sciences · 2026Article
- Detecting differential transcript usage in complex diseases with SPIT.Cell reports methods · 2024Article
- Detecting differential transcript usage in complex diseases with SPIT.bioRxiv : the preprint server for biology · 2023Article
- Article
- Alternative start and termination sites of transcription drive most transcript isoform differences across human tissues.Nucleic acids research · 2018Article
- Specific and reliable detection of Myosin 1C isoform A by RTqPCR in prostate cancer cells.PeerJ · 2018Article
- N-terminal splicing extensions of the humanThe Journal of biological chemistry · 2017Article
- Myosin isoform expressed in metastatic prostate cancer stimulates cell invasion.Scientific reports · 2017Article
- Myosin-I molecular motors at a glance.Journal of cell science · 2016Review
- Lowered Expression of Tumor Suppressor Candidate MYO1C Stimulates Cell Proliferation, Suppresses Cell Adhesion and Activates AKT.PloS one · 2016Article
- Design (and) principles of nuclear dynamics in Stockholm.Nucleus (Austin, Tex.) · 2015Article
- Selective expression of myosin IC Isoform A in mouse and human cell lines and mouse prostate cancer tissues.PloS one · 2014Article
- Mechanochemical properties of human myosin-1C are modulated by isoform-specific differences in the N-terminal extension.The Journal of biological chemistryArticle
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundMyosin IC is a single headed member of the myosin superfamily that localizes to the cytoplasm and the nucleus and is implicated in a variety of processes in both compartments. We recently identified a novel isoform of myosin IC and showed that the MYOIC gene in mammalian cells encodes three isoforms (isoforms A, B, and C) that differ only in the addition of short isoform-specific N-terminal peptides. The expression pattern of the isoforms and the mechanisms of expression regulation remain unknown.
resultsTo determine the expression patterns of myosin IC isoforms, we performed a comprehensive expression analysis of the two myosin IC isoforms (isoform A and B) that contain isoform-specific sequences. By immunoblotting with isoform-specific antibodies and by qRT-PCR with isoform-specific primer we demonstrate that myosin IC isoforms A and B have distinct expression patterns in mouse tissues. Specifically, we show that myosin IC isoform A is expressed in a tissue specific pattern, while myosin IC isoform B is ubiquitously expressed at comparable levels in mouse tissues.
conclusionsThe differences in the expression profile of the myosin IC isoforms indicate a tissue-specific MYOIC gene regulation and further suggest that the myosin IC isoforms, despite their high sequence homology, might have tissue-specific and isoform-specific functions.
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