Cathepsins as transcriptional activators?
One action of proteases is limited cleavage of latent transcription factors, releasing active factors to initiate nuclear signaling. Goulet et al., in a recent Molecular Cell paper, provide evidence that a lysosomal protease, cathepsin L, exists in a previously unsuspected isoform capable of trafficking to the nucleus and activating the CDP/Cux transcription factor. The findings should stimulate new research on the nature of nuclear proteases involved in signaling.
Chapman
Harold A
HA
Department of Medicine and Cardiovascular Research Institute, University of California, San Francisco, 513 Parnassus Avenue, HSE-201, San Francisco, CA 94143, USA.
D021581:Active Transport, Cell Nucleus / Q000502:physiology; D000818:Animals; D056668:Cathepsin L; D002403:Cathepsins / Q000378:metabolism*; D002467:Cell Nucleus / Q000378:metabolism*; D003546:Cysteine Endopeptidases; D018398:Homeodomain Proteins; D006801:Humans; D008247:Lysosomes / Q000378:metabolism*; D009687:Nuclear Proteins / Q000378:metabolism; D012097:Repressor Proteins / Q000378:metabolism; D014157:Transcription Factors; D015533:Transcriptional Activation / Q000502:physiology*
C080632:CUX1 protein, human; D018398:Homeodomain Proteins; D009687:Nuclear Proteins; D012097:Repressor Proteins; D014157:Transcription Factors; D002403:Cathepsins; D003546:Cysteine Endopeptidases; C534281:CTSL protein, human; D056668:Cathepsin L