Juxtaposition of CNR Protocadherins and Reelin Expression in the Developing Spinal Cord

Carroll, Patrick; Gayet, Odile; Feuillet, Christian; Kallenbach, Sacha; Bovis, Béatrice de; Dudley, Keith; Alonso, Serge

doi:10.1006/mcne.2001.0966

Cited by 56 publications

(43 citation statements)

References 33 publications

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“…Ret autophosphorylation and subsequent downstream signaling are activated by binding to a complex consisting of a glial cell line-derived neurotrophic factor (GDNF) family ligand and a glycosyl-phosphatidyl inositol (GPI)-anchored co-receptor of the GDNF receptor alpha (GFRα) family. Interestingly, Pcdhα is expressed at high levels in most tissues in which Ret plays an important cellular role, including MNs and sensory and sympathetic ganglia (21,22). In addition, both the Pcdhs and Ret contain conserved cadherin-like extracellular domains (2,23).…”

Section: Identification Of Proteins That Interact With Pcdhα4 Using Tmentioning

confidence: 99%

“…Next, we asked whether the interactions between Pcdhα or Pcdhγ and Ret and phosphorylation of the Pcdhs by Ret are general regulatory mechanisms for Pcdhs in Ret-expressing cells in the nervous system. Because both Ret and Pcdhs are highly expressed in MNs and superior cervical ganglia (SCG) (21,22), we investigated the relationship between Ret and Pcdhs in ES cell-derived MNs and in primary sympathetic neuron cultures derived from SCGs. In agreement with our CAD cell results (Fig.…”

Section: Ret Is Required For the Phosphorylation Of Pcdhα And Pcdhγ Imentioning

confidence: 99%

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Phosphorylation of protocadherin proteins by the receptor tyrosine kinase Ret

Schalm

Ballif

Buchanan

et al. 2010

Proc. Natl. Acad. Sci. U.S.A.

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The clustered protocadherins (Pcdhs) are a large family of cadherinlike transmembrane proteins expressed in the nervous system. Stochastic expression of Pcdh genes and alternative splicing of their pre-mRNAs have the potential to generate enormous protein diversity at the cell surface of neurons. At present, the regulation and function of Pcdh proteins are largely unknown. Here, we show that Pcdhs form a heteromeric signaling complex(es), consisting of multiple Pcdh isoforms, receptor tyrosine kinases, phosphatases, and cell adhesion molecules. In particular, we find that the receptor tyrosine kinase rearranged during transformation (Ret) binds to Pcdhs in differentiated neuroblastoma cells and is required for stabilization and differentiation-induced phosphorylation of Pcdh proteins. In addition, the Ret ligand glial cell line-derived neurotrophic factor induces phosphorylation of Pcdhγ in motor neurons and phosphorylation of Pcdhα and Pcdhγ in sympathetic neurons. Conversely, Pcdh proteins are also required for the stabilization of activated Ret in neuroblastoma cells and sympathetic ganglia. Thus, Pcdhs and Ret are functional components of a phosphorylationdependent signaling complex. intracellular domain | signal transduction | TAP tag | protein-protein interactions | protein purification

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Section: Identification Of Proteins That Interact With Pcdhα4 Using Tmentioning

confidence: 99%

Section: Ret Is Required For the Phosphorylation Of Pcdhα And Pcdhγ Imentioning

confidence: 99%

Phosphorylation of protocadherin proteins by the receptor tyrosine kinase Ret

Schalm

Ballif

Buchanan

et al. 2010

Proc. Natl. Acad. Sci. U.S.A.

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“…Hybridization signal was detected using alkaline phosphatase-conjugated antibodies against digoxigenin (Roche, Mannheim, Germany) and BM purple substrate (Roche). Whole-mount embryo ISH was performed as previously described (Carroll et al, 2001, Goddard et al, 1996. Hybridization with the sense probes was performed on control embryos and serial frozen sections under the same conditions; no signal was detected in examined tissues.…”

Section: In Situ Hybridizationmentioning

confidence: 99%

Calpain 2 expression pattern and sub-cellular localization during mouse embryogenesis

Raynaud¹,

Marcilhac²,

Chébli³

et al. 2008

Int. J. Dev. Biol.

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Regulation of migration and proliferation by calpain has been shown in various cell types; however, no data are available concerning calpain 2 (CAPN2) localization in embryonic tissues. Here, we report the expression pattern of CAPN2 during mouse embryonic development. Expression of the capn2 gene is observed throughout embryonic development. From ES cells and the 8-cell stage to late neurulation stages, CAPN2 is expressed in the cytoplasm and nuclear compartments, with a clear co-localisation with chromatin. Whole-mount in situ hybridization analysis from E8.5 to 14.5 stages indicates high levels of capn2 expression in the nervous system, heart and mesodermal tissues. Up-regulation is maintained during later developmental stages in proliferating cells and in precursor cells involved in muscle (myoblasts) or bone formation (chondrocytes). At later developmental stages, elevated mRNA levels coincided with CAPN2 nuclear localization in these cell types, while differentiated cells maintained cytoplasmic expression. This detailed analysis reveals dynamic expression: nuclear localization was associated either with active cell mitosis in embryonic stem cells and early developmental stages or with precursor cells later during organogenesis. Thus, these data indicate that CAPN2 may represent a key factor in development from the first cell division.

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“…In situ hybridization (ISH) on whole-mount preparation and cryostat sections were carried out as described by Carroll et al (Carroll et al, 2001). ISH on vibratome sections has been described previously (Poluch et al, 2003).…”

Section: In Situ Hybridization and Immunohistochemistrymentioning

confidence: 99%

Reelin signaling is necessary for a specific step in the migration of hindbrain efferent neurons

et al. 2005

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The cytoarchitecture of the hindbrain results from precise and co-ordinated sequences of neuronal migrations. Here, we show that reelin, an extracellular matrix protein involved in neuronal migration during CNS development, is necessary for an early, specific step in the migration of several hindbrain nuclei. We identified two cell populations not previously known to be affected in reeler mutants that show a common migratory defect: the olivocochlear efferent neurons and the facial visceral motor nucleus. In control embryos, these cells migrate first toward a lateral position within the neural tube, and then parallel to the glial cell processes, to a ventral position where they settle close to the pial surface. In reelermutants, the first migration is not affected, but the neurons are unable to reach the pial surface and remain in an ectopic position. Indeed, this is the first evidence that the migration of specific hindbrain nuclei can be divided into two parts: a reelin-independent and a reelin-dependent migration. We also show that reelin is expressed at high levels at the final destination of the migratory process, while the reelin intracellular effector Dab1 was expressed by cell groups that included the two populations affected. Mice mutant at the Dab1 locus, called scrambler, exhibit the same phenotype, a failure of final migration. However, examination of mice lacking both reelin receptors, ApoER2 and VLDLR, did not reveal the same phenotype, suggesting involvement of an additional reelin-binding receptor. In the hindbrain, reelin signaling might alter the adhesive properties of efferent neurons and their ability to respond to directional cues, as has been suggested for the migration of olfactory bulb precursors.

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Juxtaposition of CNR Protocadherins and Reelin Expression in the Developing Spinal Cord

Cited by 56 publications

References 33 publications

Phosphorylation of protocadherin proteins by the receptor tyrosine kinase Ret

Phosphorylation of protocadherin proteins by the receptor tyrosine kinase Ret

Calpain 2 expression pattern and sub-cellular localization during mouse embryogenesis

Reelin signaling is necessary for a specific step in the migration of hindbrain efferent neurons

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