Filamin A-interacting protein (FILIP) regulates cortical cell migration out of the ventricular zone

Nagano, Takashi; Yoneda, Takunari; Hatanaka, Yasuo; Kubota, Chikara; Murakami, Fujio; Sato, Makoto

doi:10.1038/ncb808

Cited by 126 publications

(124 citation statements)

References 29 publications

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“…Several in utero experiments have revealed a role for LIS1 , DCX (Bai et al, 2003), CDK5 (Ohshima et al, 2007), and Filamin A (Flna) (Nagano et al, 2002(Nagano et al, , 2004 in the regulation of the multipolar stage. Here, we have shown two means to rescue neurons stalled in the multipolar stage.…”

Section: Discussionmentioning

confidence: 99%

Accurate Balance of the Polarity Kinase MARK2/Par-1 Is Required for Proper Cortical Neuronal Migration

Sapir¹,

Sapoznik²,

Levy³

et al. 2008

J. Neurosci.

103

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Radial neuronal migration is key in structuring the layered cortex. Here we studied the role of MARK2/Par-1 in this process. The dual name stands for the MAP/microtubule affinity-regulating kinase 2 (MARK2) and the known polarity kinase 1 (Par-1). Reduced MARK2 levels using in utero electroporation resulted in multipolar neurons stalled at the intermediate zone border. Reintroduction of the wild-type kinase postmitotically improved neuronal migration. Our results indicated that reduction in MARK2 affected centrosomal dynamics in migrating neurons of the cerebral cortex. Increased MARK2 has been shown to destabilize microtubules, and here we show for the first time that reduced MARK2 stabilized microtubules in primary cultured neurons. Kinase-independent activity permitted multipolar-to-bipolar transition but did not restore proper migration. Increased MARK2 levels resulted in a different phenotype, which is loss of neuronal polarity. MARK2 kinase activity reduction hindered migration in the developing brain, which was rescued by increasing kinase activity. Our results stress the necessity of maintaining dynamic microtubules for proper neuronal migration. Furthermore, the exact requirements for MARK2 and its kinase activity vary during the course of neuronal migration. Collectively, our results stress the requirements for the different roles of MARK2 during neuronal migration.

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Section: Discussionmentioning

confidence: 99%

Accurate Balance of the Polarity Kinase MARK2/Par-1 Is Required for Proper Cortical Neuronal Migration

Sapir¹,

Sapoznik²,

Levy³

et al. 2008

J. Neurosci.

103

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“…FLNa interacting protein (FILIP), ribosomal S6 kinase, protein kinase C␣, and GTPases of the Rho-and Rac-families, which thereby implicate FLNa in cell shape modulation and integrindependent adhesion and motility (Nagano et al, 2002;Ohta et al, 1999;Tigges et al, 2003;Woo et al, 2004). GTPases have the extraordinary ability to remodel actin-based cytoskeletal structures.…”

Section: Discussionmentioning

confidence: 99%

CEACAM1 functionally interacts with filamin A and exerts a dual role in the regulation of cell migration

Klaile

Kannicht³

et al. 2005

Journal of Cell Science

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The carcinoembryonic antigen-related cell adhesion molecule CEACAM1 (CD66a) and the scaffolding protein filamin A have both been implicated in tumor cell migration. In the present study we identified filamin A as a novel binding partner for the CEACAM1-L cytoplasmic domain in a yeast two-hybrid screen. Direct binding was shown by surface plasmon resonance analysis and by affinity precipitation assays. The association was shown for human and rodent CEACAM1-L in endogenous CEACAM1-L expressing cells. To address functional aspects of the interaction, we used a well-established melanoma cell system. We found in different migration studies that the interaction of CEACAM1-L and filamin A drastically reduced migration and cell scattering, whereas each of these proteins when expressed alone, acted promigratory. CEACAM1-L binding to filamin A reduced the interaction of the latter with RalA, a member of the Ras-family of GTPases. Furthermore, co-expression of CEACAM1-L and filamin A led to a reduced focal adhesion turnover. Independent of the presence of filamin A, the expression of CEACAM1-L led to an increased phosphorylation of focal adhesions and to altered cytoskeletal rearrangements during monolayer wound healing assays. Together, our data demonstrate a novel mechanism for how CEACAM1-L regulates cell migration via its interaction with filamin A.

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“…This was further supported by indications that FLNa-deficiency impaired neuronal migration (Fox and Walsh, 1999;Nagano et al, 2002). Further studies based on knockout mice (Hart et al, 2006;Feng et al, 2006) and the use of small interference RNA showed that while in many settings loss of only one FLN isoform is not sufficient to impair migration, loss of two or more FLNs impaired initiation of migration and cell spreading Lynch et al, 2011;Heuzé et al, 2008).…”

Section: Introductionmentioning

confidence: 89%

Filamin A controls matrix metalloprotease activity and regulates cell invasion in human fibrosarcoma cells.

Baldassarre

Razinia

Brahme

et al. 2012

Journal of Cell Science

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SummaryFilamins are an important family of actin-binding proteins that, in addition to bundling actin filaments, link cell surface adhesion proteins, signaling receptors and channels to the actin cytoskeleton, and serve as scaffolds for an array of intracellular signaling proteins. Filamins are known to regulate the actin cytoskeleton, act as mechanosensors that modulate tissue responses to matrix density, control cell motility and inhibit activation of integrin adhesion receptors. In this study, we extend the repertoire of filamin activities to include control of extracellular matrix (ECM) degradation. We show that knockdown of filamin increases matrix metalloproteinase (MMP) activity and induces MMP2 activation, enhancing the ability of cells to remodel the ECM and increasing their invasive potential, without significantly altering two-dimensional random cell migration. We further show that within filamin A, the actin-binding domain is necessary, but not sufficient, to suppress the ECM degradation seen in filamin-A-knockdown cells and that dimerization and integrin binding are not required. Filamin mutations are associated with neuronal migration disorders and a range of congenital malformations characterized by skeletal dysplasia and various combinations of cardiac, craniofacial and intestinal anomalies. Furthermore, in breast cancers loss of filamin A has been correlated with increased metastatic potential. Our data suggest that effects on ECM remodeling and cell invasion should be considered when attempting to provide cellular explanations for the physiological and pathological effects of altered filamin expression or filamin mutations.

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Filamin A-interacting protein (FILIP) regulates cortical cell migration out of the ventricular zone

Cited by 126 publications

References 29 publications

Accurate Balance of the Polarity Kinase MARK2/Par-1 Is Required for Proper Cortical Neuronal Migration

Accurate Balance of the Polarity Kinase MARK2/Par-1 Is Required for Proper Cortical Neuronal Migration

CEACAM1 functionally interacts with filamin A and exerts a dual role in the regulation of cell migration

Filamin A controls matrix metalloprotease activity and regulates cell invasion in human fibrosarcoma cells.

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