Journal
CELL
Volume 127, Issue 1, Pages 45-48Publisher
CELL PRESS
DOI: 10.1016/j.cell.2006.09.013
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Funding
- NCI NIH HHS [R01-CA096768, R01-CA079992] Funding Source: Medline
- NIAMS NIH HHS [R01-AR051448, R01-AR051889] Funding Source: Medline
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The role of receptor tyrosine kinases (RTKs) in transmembrane signaling is well established. Recently, ligand-dependent translocation of RTKs to the nucleus has been reported, but the functional importance of this process remains unclear. In this issue, Sardi et al. (2006) provide evidence for direct signaling in the nucleus by an intracellular ErbB4 receptor fragment that is released upon receptor activation by ligand. The fragment forms a complex with the adaptor TAB2 and the corepressor N-CoR and transits to the nucleus, where it represses transcription of genes that promote the formation of astrocytes.
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