Identification of neurabin II as a novel doublecortin interacting protein

Tsukada, Miki; Prokscha, Alexander; Oldekamp, Judit; Eichele, Gregor

doi:10.1016/s0925-4773(03)00177-1

Cited by 62 publications

(54 citation statements)

References 39 publications

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“…Nevertheless, some results implicated an interaction of DCX with the actin cytoskeleton, directly or via Neurabin 2. 19,20 Interestingly, BAC26042 and, to some extent the DCX domains of DCLK2 localized to the cell periphery, at sites reminiscent of lamellipodia (Fig. 5E-H and Fig.…”

Section: Resultsmentioning

confidence: 97%

“…However, although neurabin 2 regulates the interaction of DCX with actin, DCX has the capability of directly interacting with actin and affecting its polymerization. 19,20 It is possible that additional DCX proteins interact directly with actin, alternatively additional mediators and regulators may exist.…”

Section: Discussionmentioning

confidence: 99%

“…Neurabin 2 connects DCX to actin microfilaments. 19,20 In addition, neurabin 2 binds to protein phosphates 1 (PP1), thereby regulating site-specific dephosphorylation of DCX (Shmueli et al, in press). JIP1/2 (JNK Interacting Protein 1 or 2) acts as a scaffold for both DCX and one of the kinases that phosphorylates it: JNK (cJun-N-terminal Kinase).…”

Section: Introductionmentioning

confidence: 99%

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The DCX Superfamily 1: Common and Divergent Roles for Members of the Mouse DCX Superfamily

Coquelle¹,

Levy²,

Bergmann³

et al. 2006

Cell Cycle

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The doublecortin-like (DCX) domains serve as protein-interaction platforms. DCX tandem domains appear in the product of the X-linked doublecortin (DCX) gene, in retinitis pigmentosa-1 (RP1), as well as in other gene products. Mutations in the human DCX gene are associated with abnormal neuronal migration, epilepsy, and mental retardation; mutations in RP1 are associated with a form of inherited blindness, while DCDC2 has been associated with dyslectic reading disabilities. Motivated by the possible importance of this gene family, a thorough analysis to detect all family members in the mouse was conducted. The DCX-repeat gene superfamily is composed of eleven paralogs, and we cloned the DCX domains from nine different genes. Our study questioned which functions attributed to the DCX domain, are conserved among the different members. Our results suggest that the proteins with the DCX-domain have conserved and unique roles in microtubule regulation and signal transduction. All the tested proteins stimulated microtubule assembly in vitro. Proteins with tandem repeats stabilized the microtubule cytoskeleton in transfected cells, while those with single repeats localized to actin-rich subcellular structures, or the nucleus. All tested proteins interacted with components of the JNK/MAP-kinase pathway, while only a subset interacted with Neurabin 2, and a nonoverlapping group demonstrated actin association. The sub-specialization of some members due to confined intracellular localization, and protein interactions may explain the success of this superfamily.

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Section: Resultsmentioning

confidence: 97%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

The DCX Superfamily 1: Common and Divergent Roles for Members of the Mouse DCX Superfamily

Coquelle¹,

Levy²,

Bergmann³

et al. 2006

Cell Cycle

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“…Doublecortin (DCX) is a microtubule-associated protein that can induce microtubule polymerization and stabilize microtubules filaments. Immunoprecipitation experiments with brain extracts showed that Spn and DCX interact incultured cells (Tsukada et al, 2003). In vitro assays showed that DCX also binds to and bundles F-actin, suggesting that the protein crosslinks microtubules and F-actin.…”

Section: -The Spinophilin Interactomementioning

confidence: 99%

“…Thus, an emerging notion is that Spn and neurabin 1 may differentially affect their target proteins and perform quite distinctive function in cell. Morphological studies have established that Spn is enriched at plasma membrane of cells although the protein is also expressed widely throughout the cytoplasm (Smith et al, 1999;Richman et al, 2001;Tsukada et al, 2003). Spn, which is expressed partly in the nucleus in mammalian cells, interacts in vitro and in vivo with the tumor-suppressor ARF (Alternative Reading Frame).…”

Section: -Introductionmentioning

confidence: 99%

The tumour suppressor function of the scaffolding protein spinophilin

Sarrouilhe¹,

Ladevèze²

2014

Atlas of Genetics and Cytogenetics in Oncology and Haematology

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Spinophilin is a scaffolding protein with modular domains that govern its interaction with a large number of cellular proteins. The Spinophilin gene locus is localized at chromosome 17q21, a chromosomal region frequently affected by genomic instability in different human tumours. The scaffolding protein interacts with the tumour-suppressor ARF which has suggested a role for Spinophilin in cell growth. More recently, in vitro and in vivo studies demonstrated that Spinophilin is a new tumour suppressor acting via the regulation of pRb. A clear downregulation of Spinophilin is found in several human cancer types. Moreover, Spinophilin loss is associated with a poor patient prognosis in carcinoma. Currently, there are controversial findings regarding a functional relationship between Spinophilin and p53 in cell cycle regulation and in carcinogenesis. Here we present the available data regarding Spinophilin function as a tumour suppressor.

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Expression of doublecortin (DCX) and doublecortin‐like kinase (DCLK) within the developing chick brain

Capes‐Davis

Tolhurst

Dunn

et al. 2004

Developmental Dynamics

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Doublecortin (DCX) is a microtubule-associated protein widely expressed in the developing mammalian nervous system and important for neuronal migration. DCX is known to belong to a novel protein family defined by sequence homology and the presence of a conserved microtubule-binding domain, but the functions of other members of this family are still undefined. In this study, we describe the cloning of the chick ortholog of doublecortin-like kinase (DCLK), a member of this family, and assess the expression of DCX and DCLK in the layered regions of the developing chick brain. DCX and DCLK are widely expressed in pallial and subpallial structures, including the telencephalon, optic tectum, and cerebellum, in similar distribution patterns. In addition to their expression in migrating cells, both proteins were also detected in the ventricular zone and in postmigratory Purkinje cells. Finally, DCX and DCLK were found to be coexpressed in all areas examined. In postmigratory Purkinje cells, DCX and DCLK both colocalized to the cell membrane, although DCLK was also distributed more generally throughout the cell soma. These data are consistent with multiple roles for DCX and DCLK in the developing chicken brain and suggest that the chick cerebellum will be an intriguing system to explore the effects of DCX and DCLK on postmigratory neuronal function. Developmental Dynamics 232:457-467, 2005.

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Identification of neurabin II as a novel doublecortin interacting protein

Cited by 62 publications

References 39 publications

The DCX Superfamily 1: Common and Divergent Roles for Members of the Mouse DCX Superfamily

The DCX Superfamily 1: Common and Divergent Roles for Members of the Mouse DCX Superfamily

The tumour suppressor function of the scaffolding protein spinophilin

Expression of doublecortin (DCX) and doublecortin‐like kinase (DCLK) within the developing chick brain

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