Speed control for neuronal migration in the postnatal brain by Gmip-mediated local inactivation of RhoA

Ota, Haruko; Hikita, Takao; Sawada, Masato; Nishioka, Tomoki; Matsumoto, Mami; Komura, Masayuki; Ohno, Akihisa; Kamiya, Yukiyo; Miyamoto, Takuya; Asai, Naoya; Enomoto, Atsushi; Takahashi, Masahide; Kaibuchi, Kozo; Sobue, Kazuya; Sawamoto, Kazunobu

doi:10.1038/ncomms5532

Cited by 48 publications

(58 citation statements)

References 61 publications

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“…This correspondence may signal an analogous functional dependence on phosphoinositides in the related functions of these yeast and mammalian Rho-GAPs that have been documented in the secretory pathway (Johnson et al, 2012; Lefèbvre et al, 2012). Gmip has also been reported to play important roles in cortical actin remodeling in early mitosis (Andrieu et al, 2014) and the speed of neuronal migration in the postnatal brain (Ota et al, 2014) – both processes in which phosphoinositides are likely to play an important regulatory role.…”

Section: Resultsmentioning

confidence: 99%

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: 99%

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

et al. 2015

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“…1C) [4]. Although many investigators have been engaged in studying the mechanism of the chain migration of SVZ neuroblasts, a complete picture of how they form a chain-like organization is far from complete [20,21]. A recent report has suggested that the retrograde flow of N-cadherin along the intercellular adhesion sites and its recycling are critical for the collective migration of astrocytes [22].…”

Section: Discussionmentioning

confidence: 96%

Potential involvement of kinesin-1 in the regulation of subcellular localization of Girdin

Muramatsu

Enomoto

Kato

et al. 2015

Biochemical and Biophysical Research Communications

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“…The same site was revealed in human protein Gmip [58], which activates RhoA GTPase and plays a crucial role in cortical actin rearrangement during early mitosis [59] and in neuronal migration [60]. In both processes, phosphoinositides are important regulators.…”

Section: Introductionmentioning

confidence: 91%

The Role of BAR Domain Proteins in the Regulation of Membrane Dynamics

2016

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Many cellular processes are associated with membrane remodeling. The BAR domain protein family plays a key role in the formation and detection of local membrane curvatures and in attracting other proteins, including the regulators of actin dynamics. Based on their structural and phylogenetic properties, BAR domains are divided into several groups which affect membrane in various ways and perform different functions in cells. However, recent studies have uncovered evidence of functional differences even within the same group. This review discusses the principles underlying the interactions of different groups of BAR domains, and their individual representatives ,with membranes.

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Speed control for neuronal migration in the postnatal brain by Gmip-mediated local inactivation of RhoA

Cited by 48 publications

References 61 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

Potential involvement of kinesin-1 in the regulation of subcellular localization of Girdin

The Role of BAR Domain Proteins in the Regulation of Membrane Dynamics

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