scholarly journals Actin-Capping Protein and the Hippo pathway regulate F-actin and tissue growth in Drosophila

2011 ◽  
Vol 124 (11) ◽  
pp. e1-e1 ◽  
Author(s):  
B. G. Fernandez ◽  
P. Gaspar ◽  
C. Bras-Pereira ◽  
B. Jezowska ◽  
S. R. Rebelo ◽  
...  
Keyword(s):  
Hippo Pathway ◽  
Tissue Growth ◽  
Capping Protein ◽  
Actin Capping Protein ◽  
The Hippo Pathway ◽  
Actin Capping

scholarly journals Actin-Capping Protein and the Hippo pathway regulate F-actin and tissue growth in Drosophila

Development ◽  
2011 ◽  
Vol 138 (11) ◽  
pp. 2337-2346 ◽  
Author(s):  
B. G. Fernandez ◽  
P. Gaspar ◽  
C. Bras-Pereira ◽  
B. Jezowska ◽  
S. R. Rebelo ◽  
...  
Keyword(s):  
Hippo Pathway ◽  
Tissue Growth ◽  
Capping Protein ◽  
Actin Capping Protein ◽  
The Hippo Pathway ◽  
Actin Capping

scholarly journals Homeostasis of theDrosophilaadult retina by Actin-Capping Protein and the Hippo pathway

2011 ◽  
Vol 4 (5) ◽  
pp. 612-615 ◽  
Author(s):  
Catarina Brás-Pereira ◽  
Tianyi Zhang ◽  
Francesca Pignoni ◽  
Florence Janody
Keyword(s):  
Hippo Pathway ◽  
Capping Protein ◽  
Actin Capping Protein ◽  
The Hippo Pathway ◽  
Actin Capping

Structural insights into the regulation of actin capping protein by twinfilin C-terminal tail

2021 ◽  
pp. 166891
Author(s):  
Shuichi Takeda ◽  
Ryotaro Koike ◽  
Ikuko Fujiwara ◽  
Akihiro Narita ◽  
Makoto Miyata ◽  
...  
Keyword(s):  
Capping Protein ◽  
Actin Capping Protein ◽  
Actin Capping ◽  
Structural Insights

scholarly journals CapZ integrates several signaling pathways in response to mechanical stiffness

2019 ◽  
Vol 151 (5) ◽  
pp. 660-669 ◽  
Author(s):  
Christopher Solís ◽  
Brenda Russell
Keyword(s):  
Mechanical Load ◽  
Phosphorylation Site ◽  
Tight Binding ◽  
Neonatal Rat ◽  
Actin Binding ◽  
Mechanical Stimuli ◽  
Muscle Adaptation ◽  
Capping Protein ◽  
Actin Capping Protein ◽  
Actin Capping

Muscle adaptation is a response to physiological demand elicited by changes in mechanical load, hormones, or metabolic stress. Cytoskeletal remodeling processes in many cell types are thought to be primarily regulated by thin filament formation due to actin-binding accessory proteins, such as the actin-capping protein. Here, we hypothesize that in muscle, the actin-capping protein (named CapZ) integrates signaling by a variety of pathways, including phosphorylation and phosphatidylinositol 4,5-bisphosphate (PIP2) binding, to regulate muscle fiber growth in response to mechanical load. To test this hypothesis, we assess mechanotransduction signaling that regulates muscle growth using neonatal rat ventricular myocytes cultured on substrates with the stiffness of the healthy myocardium (10 kPa), fibrotic myocardium (100 kPa), or glass. We investigate how PIP2 signaling affects CapZ using the PIP2 sequestering agent neomycin and the effect of PKC-mediated CapZ phosphorylation using the PKC-activating drug phorbol 12-myristate 13-acetate (PMA). Molecular simulations suggest that close interactions between PIP2 and the β-tentacle of CapZ are modified by phosphorylation at T267. Fluorescence recovery after photobleaching (FRAP) demonstrates that the kinetic binding constant of CapZ to sarcomeric thin filaments in living muscle cells increases with stiffness or PMA treatment but is diminished by PIP2 reduction. Furthermore, CapZ with a deletion of the β-tentacle that lacks the phosphorylation site T267 shows increased FRAP kinetics with lack of sensitivity to PMA treatment or PIP2 reduction. Förster resonance energy transfer (FRET) probes the molecular interactions between PIP2 and CapZ, which are decreased by PIP2 availability or by the β-tentacle truncation. These data suggest that CapZ is bound to actin tightly in the idle, locked state, with little phosphorylation or PIP2 binding. However, this tight binding is loosened in growth states triggered by mechanical stimuli such as substrate stiffness, which may have relevance to fibrotic heart disease.

scholarly journals The palmitoyltransferase Approximated promotes growth via the Hippo pathway by palmitoylation of Fat

2016 ◽  
Vol 216 (1) ◽  
pp. 265-277 ◽  
Author(s):  
Hitoshi Matakatsu ◽  
Seth S. Blair ◽  
Richard G. Fehon
Keyword(s):  
Posttranslational Modification ◽  
Hippo Pathway ◽  
Growth Control ◽  
Tissue Growth ◽  
Negative Regulator ◽  
Pathway Activity ◽  
Protein Association ◽  
Junctional Region ◽  
Growth Loss ◽  
The Hippo Pathway

The large protocadherin Fat functions to promote Hippo pathway activity in restricting tissue growth. Loss of Fat leads to accumulation of the atypical myosin Dachs at the apical junctional region, which in turn promotes growth by inhibiting Warts. We previously identified Approximated (App), a DHHC domain palmitoyltransferase, as a negative regulator of Fat signaling in growth control. We show here that App promotes growth by palmitoylating the intracellular domain of Fat, and that palmitoylation negatively regulates Fat function. Independently, App also recruits Dachs to the apical junctional region through protein–protein association, thereby stimulating Dachs’s activity in promoting growth. Further, we show that palmitoylation by App functions antagonistically to phosphorylation by Discs-overgrown, which activates Fat. Together, these findings suggest a model in which App promotes Dachs activity by simultaneously repressing Fat via posttranslational modification and recruiting Dachs to the apical junctional region, thereby promoting tissue growth.

scholarly journals Want to promote tissue growth? There’s an App for that!

2016 ◽  
Vol 216 (1) ◽  
pp. 1-1 ◽  
Author(s):  
Ben Short
Keyword(s):  
Hippo Pathway ◽  
Tissue Growth ◽  
The Hippo Pathway

Study describes how a palmitoyltransferase regulates the Hippo pathway in flies.

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