The F-BAR protein family

Fricke, Robert; Gohl, Christina; Bogdan, Sven

doi:10.4161/cib.3.2.10521

Cited by 18 publications

(14 citation statements)

References 65 publications

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“…93 In addition, BAR proteins can recruit actin and actin regulators like WASP/WAVE to the membrane which facilitates the protrusion of the membrane. I-Bar (inverted BAR) domain bearing proteins such as Irs-58 were proposed to regulate neurite formation and growth by inducing negative curvature and filopodia.…”

Section: Building a Growth Cone-actinmentioning

confidence: 99%

The cytoskeleton and neurite initiation

2013

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Neurons begin their life as simple spheres, but can ultimately assume an elaborate morphology with numerous, highly arborized dendrites, and long axons. This is achieved via an astounding developmental progression which is dependent upon regulated assembly and dynamics of the cellular cytoskeleton. As neurites emerge out of the soma, neurons break their spherical symmetry and begin to acquire the morphological features that define their structure and function. Neurons regulate their cytoskeleton to achieve changes in cell shape, velocity, and direction as they migrate, extend neurites, and polarize. Of particular importance, the organization and dynamics of actin and microtubules directs the migration and morphogenesis of neurons. This review focuses on the regulation of intrinsic properties of the actin and microtubule cytoskeletons and how specific cytoskeletal structures and dynamics are associated with the earliest phase of neuronal morphogenesis—neuritogenesis.

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Section: Building a Growth Cone-actinmentioning

confidence: 99%

The cytoskeleton and neurite initiation

2013

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“…A molecular link between the membrane and actin dynamics is provided by proteins of the F-BAR family, such as Cip4/Toca-1 (Heath and Insall, 2008; Robertson et al, 2009; Aspenström, 2010; Fricke et al, 2010). Cip4/Toca-1 binds to membranes with high curvature and recruits activators of the Arp2/3 complex such as SCAR/WAVE and WASP with its C-terminal SH3 domain to promote local accumulation of branched actin filaments (Fricke et al, 2009).…”

Section: Introductionmentioning

confidence: 99%

The F-BAR protein Cip4/Toca-1 antagonizes the formin Diaphanous in membrane stabilization and compartmentalization

Yan

Winterhoff

et al. 2013

Journal of Cell Science

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SummaryDuring Drosophila embryogenesis, the first epithelium with defined cortical compartments is established during cellularization. Actin polymerization is required for the separation of lateral and basal domains as well as suppression of tubular extensions in the basal domain. The actin nucleator mediating this function is unknown. We found that the formin Diaphanous (Dia) is required for establishing and maintaining distinct lateral and basal domains during cellularization. In dia mutant embryos lateral marker proteins, such as Discs-large and Armadillo/β-Catenin spread into the basal compartment. Furthermore, high-resolution and live-imaging analysis of dia mutant embryos revealed an increased number of membrane extensions and endocytic activity at the basal domain, indicating a suppressing function of dia on membrane invaginations. Dia function might be based on an antagonistic interaction with the F-BAR protein Cip4/Toca-1, a known activator of the WASP/WAVE-Arp2/3 pathway. Dia and Cip4 physically and functionally interact and overexpression of Cip4 phenocopies dia loss-of-function. In vitro, Cip4 inhibits mainly actin nucleation by Dia. Thus, our data support a model in which linear actin filaments induced by Dia stabilize cortical compartmentalization by antagonizing membrane turnover induced by WASP/WAVE-Arp2/3.

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“…Recent live-imaging analyses of dia mutant embryos revealed an increased endocytic activity and thus suggests an inhibitory function of Dia on tubular membrane invaginations. This inhibitory role of Dia is based on an antagonistic interaction with the F-BAR protein Cip4, a known activator of the WASP/WAVE-Arp2/3 pathway 22 , 90 - 92 . Since Cip4 inhibits actin nucleation by Dia in vitro, a model has been proposed in which Cip4 controls 2 different pools of actin filaments: activation of branched filaments by its WASP/WAVE interaction and suppression of linear filaments by inhibition of Dia 22 .…”

Section: Introductionmentioning

confidence: 99%

Formin’ cellular structures

Bogdan

Schultz

Großhans

2013

Communicative & Integrative Biology

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Members of the Diaphanous (Dia) protein family are key regulators of fundamental actin driven cellular processes, which are conserved from yeast to humans. Researchers have uncovered diverse physiological roles in cell morphology, cell motility, cell polarity, and cell division, which are involved in shaping cells into tissues and organs. The identification of numerous binding partners led to substantial progress in our understanding of the differential functions of Dia proteins. Genetic approaches and new microscopy techniques allow important new insights into their localization, activity, and molecular principles of regulation.

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The F-BAR protein family

Cited by 18 publications

References 65 publications

The cytoskeleton and neurite initiation

The cytoskeleton and neurite initiation

The F-BAR protein Cip4/Toca-1 antagonizes the formin Diaphanous in membrane stabilization and compartmentalization

Formin’ cellular structures

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