FCH/Cdc15 domain determines distinct subcellular localization of NOSTRIN

Icking, Ann; Schilling, Kirstin; Wiesenthal, Anja; Opitz, Nils; Müller‐Esterl, Werner

doi:10.1016/j.febslet.2005.11.078

Cited by 19 publications

(15 citation statements)

References 19 publications

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“…The membrane tubulation by the Rgd1p F-BAR domain in HeLa cells resembles that seen for most mammalian F-BAR domains, including those from FBP17, CIP4, FCHo1/2, pacsin 1, nostrin, and PSTPIP1/2 (Henne et al, 2010; Icking et al, 2006; Itoh and De Camilli, 2006; Itoh et al, 2005; Tsujita et al, 2006), which all bind relatively non-specifically to anionic phospholipids. The FBP17, CIP4, and pacsin 1 F-BAR domains preferentially bind PtdSer-containing membranes, and phosphoinositides typically further enhance membrane binding (Henne et al, 2010; Itoh et al, 2005; Tsujita et al, 2006).…”

Section: Resultsmentioning

confidence: 68%

Comparison of Saccharomyces cerevisiae F-BAR Domain Structures Reveals a Conserved Inositol Phosphate Binding Site

et al. 2015

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SUMMARY F-BAR domains control membrane interactions in endocytosis, cytokinesis, and cell signaling. Although generally thought to bind curved membranes containing negatively charged phospholipids, numerous functional studies argue that differences in lipid-binding selectivities of F-BAR domains are functionally important. Here, we compare membrane-binding properties of the S. cerevisiae F-BAR domains in vitro and in vivo. Whereas some F-BAR domains (such as Bzz1p and Hof1p F-BARs) bind equally well to all phospholipids, the F-BAR domain from the RhoGAP Rgd1p preferentially binds phosphoinositides. We determined X-ray crystal structures of F-BAR domains from Hof1p and Rgd1p, the latter bound to an inositol phosphate. The structures explain phospholipid-binding selectivity differences, and reveal an F-BAR phosphoinositide binding site that is fully conserved in a mammalian RhoGAP called Gmip, and is partly retained in certain other F-BAR domains. Our findings reveal previously unappreciated determinants of F-BAR domain lipid-binding specificity, and provide a basis for its prediction from sequence.

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Section: Resultsmentioning

confidence: 68%

Comparison of Saccharomyces cerevisiae F-BAR Domain Structures Reveals a Conserved Inositol Phosphate Binding Site

et al. 2015

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“…NOSTRIN, a 58kDa protein with high expression in the endothelium [69, 70], has a C terminal coiled-coil motif that may trimerize and serve as a platform for binding of several proteins [71]. Because NOSTRIN also associates with caveolin-1, it is believed that NOSTRIN-dependent movement of eNOS proceeds through a specialized endocytosis of caveolar endosomes [70].…”

Section: Regulation Of No Production: the Dynamic Modulation Of Enosmentioning

confidence: 99%

Compartmentalized nitric oxide signaling in the resistance vasculature

Mutchler¹,

Straub

2015

Nitric Oxide

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Nitric oxide (NO) was first described as a bioactive molecule through its ability to stimulate soluble guanylate cyclase, but the revelation that NO was the endothelium derived relaxation factor drove the field to its modern state. The wealth of research conducted over the past 30 years has provided us with a picture of how diverse NO signaling can be within the vascular wall, going beyond simple vasodilation to include such roles as signaling through protein S-nitrosation. This expanded view of NO’s actions requires highly regulated and compartmentalized production. Importantly, resistance arteries house multiple proteins involved in the production and transduction of NO allowing for efficient movement of the molecule to regulate vascular tone and reactivity. In this review, we focus on the many mechanisms regulating NO production and signaling action in the vascular wall, with a focus on the control of endothelial nitric oxide synthase (eNOS), the enzyme responsible for synthesizing most of the NO within these confines. We also explore how cross talk between the endothelium and smooth muscle in the microcirculation can modulate NO signaling, illustrating that this one small molecule has the capability to produce a plethora of responses.

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“…WRP and the srGAP family members have a conserved N-terminal Fes and CIP4 homology BAR-like (F-BAR) domain (Itoh et al, 2005; Aspenström, 2009). Several studies have shown this to be a lipid-binding domain that induces membrane invagination and regulates processes such as endocytosis (Takei et al, 1999; Kamioka et al, 2004; Itoh et al, 2005; Icking et al, 2006; Tsujita et al, 2006; Shimada et al, 2007). Surprisingly, a recent study of srGAP2 showed that its F-BAR domain enhances outward membrane protrusions (Guerrier et al, 2009).…”

Section: Introductionmentioning

confidence: 99%

WRP/srGAP3Facilitates the Initiation of Spine Development by an Inverse F-BAR Domain, and Its Loss Impairs Long-Term Memory

Carlson¹,

Lloyd²,

Kruszewski³

et al. 2011

J. Neurosci.

110

147

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The WAVE-associated Rac GAP, WRP, is thought to regulate key aspects of synapse development and function and may be linked to mental retardation in humans. WRP contains a newly described inverse F-BAR (IF-BAR) domain of unknown function. Our studies show that this domain senses/facilitates outward protrusions analogous to filopodia and that the molecular basis for this is likely explained by a convex lipid-binding surface on the WRP IF-BAR domain. In dendrites the IF-BAR domain of WRP forms a bud on the shaft from which precursors to spines emerge. Loss of WRP in vivo and in vitro results in reduced density of spines. In vivo this is primarily a loss of mushroom-shaped spines. Developmentally, WRP function is critical at the onset of spinogenesis, when dendritic filopodia are prevalent. Finally, because WRP is implicated in mental retardation, behaviors of WRP heterozygous and null mice have been evaluated. Results from these studies confirm that loss of WRP is linked to impaired learning and memory.

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FCH/Cdc15 domain determines distinct subcellular localization of NOSTRIN

Cited by 19 publications

References 19 publications

Comparison of Saccharomyces cerevisiae F-BAR Domain Structures Reveals a Conserved Inositol Phosphate Binding Site

Comparison of Saccharomyces cerevisiae F-BAR Domain Structures Reveals a Conserved Inositol Phosphate Binding Site

Compartmentalized nitric oxide signaling in the resistance vasculature

WRP/srGAP3Facilitates the Initiation of Spine Development by an Inverse F-BAR Domain, and Its Loss Impairs Long-Term Memory

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