Proteomics

Dataset Information

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An extracellular receptor tyrosine kinase motif orchestrating intracellular STAT activation


ABSTRACT: 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.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Cercopithecus Aethiops (green Monkey) (grivet) Homo Sapiens (human) Mus Musculus (mouse)

SUBMITTER: Johannes Merilahti  

LAB HEAD: Klaus Elenius

PROVIDER: PXD017783 | Pride | 2023-01-30

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
COS7_AllPeptides.psmtsv Other
COS7_AllProteinGroups.tsv Tabular
COS7_PhaL.mzML Mzml
COS7_PhaL.raw Raw
COS7_ctrl.mzML Mzml
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Publications

An extracellular receptor tyrosine kinase motif orchestrating intracellular STAT activation.

Vaparanta Katri K   Jokilammi Anne A   Tamirat Mahlet M   Merilahti Johannes A M JAM   Salokas Kari K   Varjosalo Markku M   Ivaska Johanna J   Ivaska Johanna J   Johnson Mark S MS   Elenius Klaus K  

Nature communications 20221114 1


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  ...[more]

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