scholarly journals Deubiquitylation and stabilization of ARMC5 by ubiquitin‐specific processing protease 7 (USP7) are critical for RCC proliferation

2021 ◽  
Author(s):  
Guobei Yan ◽  
Na Liu ◽  
Jun Tian ◽  
Yanli Fu ◽  
Wei Wei ◽  
...  
Keyword(s):  
Processing Protease

scholarly journals amontillado, the Drosophila Homolog of the Prohormone Processing Protease PC2, Is Required During Embryogenesis and Early Larval Development

Genetics ◽  
2003 ◽  
Vol 163 (1) ◽  
pp. 227-237 ◽  
Author(s):  
Lowell Y M Rayburn ◽  
Holly C Gooding ◽  
Semil P Choksi ◽  
Dhea Maloney ◽  
Ambrose R Kidd ◽  
...  
Keyword(s):  
Larval Development ◽  
Secretory Pathway ◽  
Larval Growth ◽  
Peptide Hormones ◽  
Complementation Group ◽  
Prohormone Processing ◽  
Complementation Groups ◽  
Regulated Secretory Pathway ◽  
Processing Protease ◽  
Larval Molt

Abstract Biosynthesis of most peptide hormones and neuropeptides requires proteolytic excision of the active peptide from inactive proprotein precursors, an activity carried out by subtilisin-like proprotein convertases (SPCs) in constitutive or regulated secretory pathways. The Drosophila amontillado (amon) gene encodes a homolog of the mammalian PC2 protein, an SPC that functions in the regulated secretory pathway in neuroendocrine tissues. We have identified amon mutants by isolating ethylmethanesulfonate (EMS)-induced lethal and visible mutations that define two complementation groups in the amon interval at 97D1 of the third chromosome. DNA sequencing identified the amon complementation group and the DNA sequence change for each of the nine amon alleles isolated. amon mutants display partial embryonic lethality, are defective in larval growth, and arrest during the first to second instar larval molt. Mutant larvae can be rescued by heat-shock-induced expression of the amon protein. Rescued larvae arrest at the subsequent larval molt, suggesting that amon is also required for the second to third instar larval molt. Our data indicate that the amon proprotein convertase is required during embryogenesis and larval development in Drosophila and support the hypothesis that AMON acts to proteolytically process peptide hormones that regulate hatching, larval growth, and larval ecdysis.

The carboxyterminal processing protease of D1 protein: expression, purification and enzymology of the recombinant and native spinach proteins

2005 ◽  
Vol 61 (7) ◽  
pp. 682-690 ◽  
Author(s):  
Bradon J Fabbri ◽  
Stephen MG Duff ◽  
Edward E Remsen ◽  
Yun-Chia Sophia Chen ◽  
John C Anderson ◽  
...  
Keyword(s):  
Protein Expression ◽  
D1 Protein ◽  
Processing Protease

scholarly journals A Genomic Cluster Containing Four Differentially Regulated Subtilisin-like Processing Protease Genes Is in Tomato Plants

1999 ◽  
Vol 274 (4) ◽  
pp. 2360-2365 ◽  
Author(s):  
Lucia Jordá ◽  
Alberto Coego ◽  
Vicente Conejero ◽  
Pablo Vera
Keyword(s):  
Tomato Plants ◽  
Processing Protease ◽  
Genomic Cluster

The carboxyterminal processing protease of D1 protein: Herbicidal activity of novel inhibitors of the recombinant and native spinach enzymes

2007 ◽  
Vol 88 (1) ◽  
pp. 1-13 ◽  
Author(s):  
Stephen M.G. Duff ◽  
Yun-Chia Sophia Chen ◽  
Brad J. Fabbri ◽  
Gopichand Yalamanchili ◽  
Bruce C. Hamper ◽  
...  
Keyword(s):  
D1 Protein ◽  
Herbicidal Activity ◽  
Processing Protease

scholarly journals Bach1 regulates self-renewal and impedes mesendodermal differentiation of human embryonic stem cells

2019 ◽  
Vol 5 (3) ◽  
pp. eaau7887 ◽  
Author(s):  
Xiangxiang Wei ◽  
Jieyu Guo ◽  
Qinhan Li ◽  
Qianqian Jia ◽  
Qing Jing ◽  
...  
Keyword(s):  
Stem Cells ◽  
Embryonic Stem Cells ◽  
Human Embryonic Stem Cells ◽  
Embryonic Stem ◽  
Gene Promoters ◽  
Lineage Specification ◽  
Self Renewal ◽  
Polycomb Repressive Complex 2 ◽  
Direct Target ◽  
Processing Protease

The transcription factor BTB and CNC homology 1 (Bach1) is expressed in the embryos of mice, but whether Bach1 regulates the self-renewal and early differentiation of human embryonic stem cells (hESCs) is unknown. We report that the deubiquitinase ubiquitin-specific processing protease 7 (Usp7) is a direct target of Bach1, that Bach1 interacts with Nanog, Sox2, and Oct4, and that Bach1 facilitates their deubiquitination and stabilization via the recruitment of Usp7, thereby maintaining stem cell identity and self-renewal. Bach1 also interacts with polycomb repressive complex 2 (PRC2) and represses mesendodermal gene expression by recruiting PRC2 to the genes’ promoters. The loss of Bach1 in hESCs promotes differentiation toward the mesendodermal germ layers by reducing the occupancy of EZH2 and H3K27me3 in mesendodermal gene promoters and by activating the Wnt/β-catenin and Nodal/Smad2/3 signaling pathways. Our study shows that Bach1 is a key determinant of pluripotency, self-renewal, and lineage specification in hESCs.

Engineering Subtilisin into a Fluoride-Triggered Processing Protease Useful for One-Step Protein Purification†

Biochemistry ◽  
2004 ◽  
Vol 43 (46) ◽  
pp. 14539-14546 ◽  
Author(s):  
Biao Ruan ◽  
Kathryn E. Fisher ◽  
Patrick A. Alexander ◽  
Viktoriya Doroshko ◽  
Philip N. Bryan
Keyword(s):  
Protein Purification ◽  
One Step ◽  
Processing Protease
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