Drosophila Cip4/Toca-1 Integrates Membrane Trafficking and Actin Dynamics through WASP and SCAR/WAVE

Fricke, Robert; Gohl, Christina; Dharmalingam, Elavarasi; Grevelhörster, Astrid; Zahedi, Baharak; Harden, Nicholas; Kessels, Michael M.; Qualmann, Britta; Bogdan, Sven

doi:10.1016/j.cub.2009.07.058

Cited by 131 publications

(187 citation statements)

References 35 publications

(43 reference statements)

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“…6C1--F, available at www.jneurosci.org as supplemental material). These results, together with a recent report that dCIP4 activates Wsp-Arp2/3-mediated actin polymerization in vitro (Fricke et al, 2009), suggest that dCIP4 acts in the Cdc42-WspArp2/3 pathway to regulate postsynaptic F-actin.…”

Section: Dcip4 Interacts With the Cdc42-wsp Pathway At The Nmj And Rementioning

confidence: 64%

“…However, our results suggest that this would not be the case. First, postsynaptic expression of a dominant-negative form of dynamin does not noticeably change extracellular Gbb levels at NMJs Second, the membrane-deforming activity of dCIP4, which has been implicated in endocytic vesicle formation (Fricke et al, 2009), is dispensable in the regulation of synaptic growth. Finally, depletion of dCIP4, Wsp, or Arp3 but not dynamin leads to an increase in the secretion of mature Gbb from cultured S2 cells, whereas dCIP4 overexpression has the opposite effect.…”

Section: And Bg57-gal4/uas-arp3mentioning

confidence: 99%

“…In the wing epithelium, Cdc42 has been shown to be required for the apical localization of dCIP4 (Fricke et al, 2009). To determine whether Cdc42 function is also required for the postsynaptic localization of dCIP4 in muscles, we analyzed NMJs of cdc42 2 , a hypomorphic allele of cdc42 (Genova et al, 2000).…”

Section: Dcip4 Is Required Postsynaptically For Normal Synaptic Growthmentioning

confidence: 99%

“…The Cdc42-and Wsp-binding activities of dCIP4, but not its membrane-tubulation activity, are essential for normal synaptic growth dCIP4 can induce membrane tubulation via its F-BAR domain (Fricke et al, 2009). In addition, the HR1 and SH3 domains of dCIP4 have been shown to interact, respectively, with the activated form of Cdc42 and its downstream effector Wsp (Leibfried et al, 2008).…”

Section: Dcip4 Is Required Postsynaptically For Normal Synaptic Growthmentioning

confidence: 99%

“…The F-BAR domain of dCIP4 has a potent activity to induce plasma membrane invagination (Fricke et al, 2009). In epithelial cells, dCIP4 has been shown to regulate dynamindependent endocytosis of E-cadherin at adherens junctions by acting downstream of Cdc42 to activate the Wsp-Arp2/3-mediated actin polymerization (Georgiou et al, 2008;Leibfried et al, 2008;Fricke et al, 2009).…”

Section: Introductionmentioning

confidence: 99%

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dCIP4 (Drosophila Cdc42-Interacting Protein 4) Restrains Synaptic Growth by Inhibiting the Secretion of the Retrograde Glass Bottom Boat Signal

Nahm

Kim²,

Paik³

et al. 2010

Journal of Neuroscience

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The bone morphogenetic protein (BMP) ligand Glass bottom boat (Gbb) acts as a retrograde growth signal at the Drosophila neuromuscular junction (NMJ). Endocytic regulation of presynaptic BMP receptors has been proposed to attenuate retrograde BMP signaling. However, it remains unknown whether the Gbb signal is also regulated by postsynaptic mechanisms. Here, we provide evidence that Drosophila Cdc42-interacting protein 4 (dCIP4) functions postsynaptically to inhibit synaptic growth. dCIP4 is localized postsynaptically at NMJs. dcip4 mutations lead to synaptic overgrowth and increased presynaptic phosphorylated mothers against decapentaplegic (Mad) levels, and these defects are rescued by muscle-specific expression of dCIP4. Biochemical and genetic analyses demonstrate that dCIP4 acts downstream of Cdc42 to activate the postsynaptic Wsp-Arp2/3 pathway. We also show that BMP signaling is necessary for synaptic overgrowth in larvae lacking postsynaptic dcip4 or wsp. Finally, dCIP4 and Wsp inhibit Gbb secretion. Thus, we propose that dCIP4 restrains synaptic growth by inhibiting postsynaptic Gbb secretion through the Wsp-Arp2/3 pathway.

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Section: Dcip4 Interacts With the Cdc42-wsp Pathway At The Nmj And Rementioning

confidence: 64%

Section: And Bg57-gal4/uas-arp3mentioning

confidence: 99%

Section: Dcip4 Is Required Postsynaptically For Normal Synaptic Growthmentioning

confidence: 99%

Section: Dcip4 Is Required Postsynaptically For Normal Synaptic Growthmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

dCIP4 (Drosophila Cdc42-Interacting Protein 4) Restrains Synaptic Growth by Inhibiting the Secretion of the Retrograde Glass Bottom Boat Signal

Nahm

Kim²,

Paik³

et al. 2010

Journal of Neuroscience

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Barfly: Sculpting membranes at the Drosophila neuromuscular junction

Robinson

2011

Developmental Neurobiology

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The ability of a cell to change the shape of its membranes is intrinsic to many cellular functions. Proteins that can alter or recognize curved membrane structures and those that can act to recruit other proteins which stabilize the membrane curvature are likely to be essential in cell functions. The BAR (Bin, amphiphysin, RVS167 homology) domain is a protein domain that can either induce lipidic membranes to curve or can sense curved membranes. BAR domains are found in several proteins at neuronal synapses. We will review BAR domain structure and the role that BAR domain containing proteins play in regulating the morphology and function of the Drosophila neuromuscular junction. In flies the BAR domain containing proteins, endophilin and syndapin affect synaptic vesicle endocytosis, whereas CIP4, dRich, nervous wreck and syndapin affect synaptic morphology. We will review the growing evidence implicating mutations in BAR domain containing proteins being the cause of human pathologies.

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Role of Bin‐Amphiphysin‐Rvs (BAR) domain proteins in mediating neuronal signaling and disease

Mallik

Bhat

Kumar

2022

Synapse

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Several proteins contain signaling domains that can regulate the cell membrane dynamics as well as the underlying cytoskeleton. Among these, Bin-Amphiphysin-Rvs (BAR) domain-containing proteins, with their membrane deforming properties, have emerged as the key players in regulating neuronal morphology and inducing neuronal signaling that can modulate synaptic architecture. While the biochemical and structural basis of membrane deformation by the BAR-domain proteins has been extensively studied, the in vivo contexts in which these proteins function remain to be elucidated. Despite the discovery of BAR-domain proteins over 25 years ago, most of the studies have primarily focused on understanding the structural and biochemical properties and cell biological processes regulated by these proteins. Understanding the functional requirements of these proteins at the level of multicellular organisms and the way these proteins regulate biological processes remains a topic of intensive study.In this review, we discuss the functional roles of BAR-domain proteins in the context of membrane dynamics and cellular signaling. We highlight recent developments describing the functional role of these proteins in neuronal morphogenesis, synaptic function, and disease.

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Drosophila Cip4/Toca-1 Integrates Membrane Trafficking and Actin Dynamics through WASP and SCAR/WAVE

Cited by 131 publications

References 35 publications

dCIP4 (Drosophila Cdc42-Interacting Protein 4) Restrains Synaptic Growth by Inhibiting the Secretion of the Retrograde Glass Bottom Boat Signal

dCIP4 (Drosophila Cdc42-Interacting Protein 4) Restrains Synaptic Growth by Inhibiting the Secretion of the Retrograde Glass Bottom Boat Signal

Barfly: Sculpting membranes at the Drosophila neuromuscular junction

Role of Bin‐Amphiphysin‐Rvs (BAR) domain proteins in mediating neuronal signaling and disease

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