Evidence for a unique RNA motif in orchestrating Orthomyxoviridae splicing
Ontology highlight
ABSTRACT:
PROVIDER: PRJNA837974 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| SRR19203101.fastq.gz | Fastqsanger.gz | |||
| SRR19203103.fastq.gz | Fastqsanger.gz | |||
| SRR19203057.fastq.gz | Fastqsanger.gz | |||
| SRR19203059.fastq.gz | Fastqsanger.gz | |||
| SRR19203061.fastq.gz | Fastqsanger.gz |
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Project description:The ErbB4 receptor isoforms JM-a and JM-b differ within their extracellular juxtamembrane (eJM) domains. Here, ErbB4 isoforms are used as a model to address the effect of structural variation in the eJM domain of receptor tyrosine kinases (RTK) on downstream signaling. A specific JM-a-like sequence motif is discovered, and its presence or absence (in JM-b-like RTKs) in the eJM domains of several RTKs is demonstrated to dictate selective STAT activation. STAT5a activation by RTKs including the JM-a like motif is shown to involve interaction with oligosaccharides of N-glycosylated cell surface proteins such as β1 integrin, whereas STAT5b activation by JM-b is dependent on TYK2. ErbB4 JM-a- and JM-b-like RTKs are shown to associate with specific signaling complexes at different cell surface compartments using analyses of RTK interactomes and super-resolution imaging. These findings provide evidence for a conserved mechanism linking a ubiquitous extracellular motif in RTKs with selective intracellular STAT signaling.
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