Cell Division Control Protein 42 Homolog

2020 ◽  
Author(s):  
Keyword(s):  
Cell Division ◽  
Control Protein ◽  
Cell Division Control

scholarly journals Severe autoinflammation in 4 patients with C-terminal variants in cell division control protein 42 homolog (CDC42) successfully treated with IL-1β inhibition

2019 ◽  
Vol 144 (4) ◽  
pp. 1122-1125.e6 ◽  
Author(s):  
Yael Gernez ◽  
Adriana A. de Jesus ◽  
Hanouf Alsaleem ◽  
Claudia Macaubas ◽  
Amitava Roy ◽  
...  
Keyword(s):  
Cell Division ◽  
Control Protein ◽  
Cell Division Control

scholarly journals The MYC-Associated Protein CDCA7 Is Phosphorylated by AKT To Regulate MYC-Dependent Apoptosis and Transformation

2012 ◽  
Vol 33 (3) ◽  
pp. 498-513 ◽  
Author(s):  
R. Montgomery Gill ◽  
Timothy V. Gabor ◽  
Amber L. Couzens ◽  
Michael P. Scheid
Keyword(s):  
Transcriptional Regulation ◽  
Cell Division ◽  
Akt Signaling ◽  
Dependent Manner ◽  
Interacting Protein ◽  
Dependent Growth ◽  
Prosurvival Kinase ◽  
Insight Into ◽  
Control Protein ◽  
Cell Division Control

ABSTRACTCell division control protein A7 (CDCA7) is a recently identified target of MYC-dependent transcriptional regulation. We have discovered that CDCA7 associates with MYC and that this association is modulated in a phosphorylation-dependent manner. The prosurvival kinase AKT phosphorylates CDCA7 at threonine 163, promoting binding to 14-3-3, dissociation from MYC, and sequestration to the cytoplasm. Upon serum withdrawal, induction of CDCA7 expression in the presence of MYC sensitized cells to apoptosis, whereas CDCA7 knockdown reduced MYC-dependent apoptosis. The transformation of fibroblasts by MYC was reduced by coexpression of CDCA7, while the non-MYC-interacting protein Δ(156–187)-CDCA7 largely inhibited MYC-induced transformation. These studies provide insight into a new mechanism by which AKT signaling to CDCA7 could alter MYC-dependent growth and transformation, contributing to tumorigenesis.

scholarly journals Septins guide microtubule protrusions induced by actin-depolymerizing toxins likeClostridium difficiletransferase (CDT)

2016 ◽  
Vol 113 (28) ◽  
pp. 7870-7875 ◽  
Author(s):  
Thilo Nölke ◽  
Carsten Schwan ◽  
Friederike Lehmann ◽  
Kristine Østevold ◽  
Olivier Pertz ◽  
...  
Keyword(s):  
Surface Plasmon Resonance ◽  
Cell Division ◽  
Clostridium Difficile ◽  
Rho Gtpases ◽  
Affinity Binding ◽  
Membrane Interaction ◽  
High Affinity Binding ◽  
High Affinity ◽  
Control Protein ◽  
Cell Division Control

HypervirulentClostridium difficilestrains, which are associated with increased morbidity and mortality, produce the actin-ADP ribosylating toxinClostridium difficiletransferase (CDT). CDT depolymerizes actin, causes formation of microtubule-based protrusions, and increases pathogen adherence. Here, we show that septins (SEPT) are essential for CDT-induced protrusion formation. SEPT2, -6, -7, and -9 accumulate at predetermined protrusion sites and form collar-like structures at the base of protrusions. The septin inhibitor forchlorfenuron or knockdown of septins inhibits protrusion formation. At protrusion sites, septins colocalize with the GTPase Cdc42 (cell division control protein 42) and its effector Borg (binder of Rho GTPases), which act as up-stream regulators of septin polymerization. Precipitation and surface plasmon resonance studies revealed high-affinity binding of septins to the microtubule plus-end tracking protein EB1, thereby guiding incoming microtubules. The data suggest that CDT usurps conserved regulatory principles involved in microtubule–membrane interaction, depending on septins, Cdc42, Borgs, and restructuring of the actin cytoskeleton.

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