Correlation between Semaphorin3A-Induced Facilitation of Axonal Transport and Local Activation of a Translation Initiation Factor Eukaryotic Translation Initiation Factor 4E

Li, Chanxia; Sasaki, Yukio; Takei, Kohtaro; Yamamoto, Hiroshi; Shouji, Masayuki; Sugiyama, Yoshifumi; Kawakami, Tadashi; Nakamura, Fumio; Yagi, Takeshi; Ohshima, Toshio; Goshima, Yoshio

doi:10.1523/jneurosci.1476-04.2004

Cited by 64 publications

(70 citation statements)

References 44 publications

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“…If the staining reflects the former case, it raises the possibility that the tyrosine phosphorylation may be involved in the regulation of axonal transport. In fact, Sema3A facilitates axonal transport, and this facilitation is blocked by a tyrosine kinase inhibitor and is attenuated in fyndeficient mouse DRG (25).…”

Section: Tyrosine Phosphorylation Site Of Crmp2 Is Tyrmentioning

confidence: 99%

Semaphorin3A Signaling Mediated by Fyn-dependent Tyrosine Phosphorylation of Collapsin Response Mediator Protein 2 at Tyrosine 32

Uchida

Ohshima

Yamashita

et al. 2009

Journal of Biological Chemistry

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Collapsin response mediator protein 2 (CRMP2) is an intracellular protein that mediates signaling of Semaphorin3A (Sema3A), a repulsive axon guidance molecule. Fyn, a Src-type tyrosine kinase, is involved in the Sema3A signaling. However, the relationship between CRMP2 and Fyn in this signaling pathway is still unknown. In our research, we demonstrated that Fyn phosphorylated CRMP2 at Tyr 32 residues in HEK293T cells. Immunohistochemical analysis using a phospho-specific antibody at Tyr 32 of CRMP showed that Tyr 32 -phosphorylated CRMP was abundant in the nervous system, including dorsal root ganglion neurons, the molecular and Purkinje cell layer of adult cerebellum, and hippocampal fimbria. Overexpression of a nonphosphorylated mutant (Tyr 32 to Phe 32 ) of CRMP2 in dorsal root ganglion neurons interfered with Sema3A-induced growth cone collapse response. These results suggest that Fyndependent phosphorylation of CRMP2 at Tyr 32 is involved in Sema3A signaling.Collapsin response mediator proteins (CRMPs) 4 have been identified as intracellular proteins that mediate Semaphorin3A (Sema3A) signaling in the nervous system (1). CRMP2 is one of the five members of the CRMP family. CRMPs also mediate signal transduction of NT3, Ephrin, and Reelin (2-4). CRMPs interact with several intracellular molecules, including tubulin, Numb, kinesin1, and Sra1 (5-8). CRMPs are involved in axon guidance, axonal elongation, cell migration, synapse maturation, and the generation of neuronal polarity (1, 2, 4, 5).CRMP family proteins are known to be the major phosphoproteins in the developing brain (1, 9). CRMP2 is phosphorylated by several Ser/Thr kinases, such as Rho kinase, cyclin-dependent kinase 5 (Cdk5), and glycogen synthase kinase 3␤ (GSK3␤) (2, 10 -13). The phosphorylation sites of CRMP2 by these kinases are clustered in the C terminus and have already been identified. Rho kinase phosphorylates CRMP2 at Thr 555 (10). Cdk5 phosphorylates CRMP2 at Ser 522 , and this phosphorylation is essential for sequential phosphorylations by GSK3␤ at Ser 518 , Thr 514 , and Thr 509 (2, 11-13). These phosphorylations disrupt the interaction of CRMP2 with tubulin or Numb (2, 3, 13). The sequential phosphorylation of CRMP2 by Cdk5 and GSK3␤ is an essential step in Sema3A signaling (11,13 (19). In dorsal root ganglion (DRG) neurons from fyn-deficient mice, Sema3A-induced growth cone collapse response is attenuated compared with control mice (19). Furthermore, we recently found that Fyn phosphorylates CRMP1 and that this phosphorylation is involved in Reelin signaling (4). Although it has been shown that CRMP2 is involved in Sema3A signaling (1,11,13), the relationship between Fyn and CRMP2 in Sema3A signaling and the tyrosine phosphorylation site(s) of CRMPs remain unknown.Here

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Section: Tyrosine Phosphorylation Site Of Crmp2 Is Tyrmentioning

confidence: 99%

Semaphorin3A Signaling Mediated by Fyn-dependent Tyrosine Phosphorylation of Collapsin Response Mediator Protein 2 at Tyrosine 32

Uchida

Ohshima

Yamashita

et al. 2009

Journal of Biological Chemistry

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“…That the required proteins, in response to physiological signals, could be translated and folded in such a short period of time is not surprising. For instance, previous work (Li et al, 2004) has shown that such a time course is plausible, because semaphorin 3A, a secreted guidance cue for growth cones, can enhance the level of phosphorylated eukaryotic translation initiation factor 4E within 5 min of its application to cultured cells.…”

Section: Possible Role Of Local Axonal Translationmentioning

confidence: 99%

The Role of Protein Synthesis in Striatal Long-Term Depression

Yin¹,

Davis²,

Ronesi³

et al. 2006

J. Neurosci.

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Long-term depression (LTD) at the corticostriatal synapse is postsynaptically induced but presynaptically expressed, the depression being a result of retrograde endocannabinoid signaling that activates presynaptic cannabinoid CB 1 receptors and reduces the probability of glutamate release. To study the role of protein synthesis in striatal LTD, we used a striatum-only preparation in which the presynaptic cell body is cut off, leaving intact only its axons, whose terminals synapse on medium spiny neurons. LTD (duration Ͼ150 min) was induced in this preparation, thus providing evidence that transcription in the presynaptic cell nucleus is not necessary for this form of plasticity. The maintenance of striatal LTD, however, was blocked by bath application of protein translation inhibitors but not by the same inhibitors loaded into the postsynaptic cell. These results suggest that local translation is critical for the expression of striatal LTD, distinguishing this form of mammalian synaptic plasticity from other forms that require postsynaptic protein synthesis. Possible roles of axonal or glial translation in striatal LTD are considered.

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“…Semaphorin3A (Sema3A) repulses axons through the coreceptor protein neuropilin-1 and plexin-As (Takahashi et al, 1999;Tamagnone et al, 1999). Sema3A functions not only as a chemorepulsive cue but also in endocytosis, facilitation of axonal transport, and spine development, and as a chemoattractive cue (Nakamura et al, 2000;Polleux et al, 2000;Goshima et al, 2002;Huber et al, 2003;Li et al, 2004;Morita et al, 2006) through the Fyn-cyclin-dependent kinase 5 (Cdk5) cascade Li et al, 2004;Morita et al, 2006). Although, how Sema3A regulates the cytoskeleton remains obscure, several intracellular molecules have been implicated as their downstream molecules.…”

Section: Introductionmentioning

confidence: 99%

Regulation of Spine Development by Semaphorin3A through Cyclin-Dependent Kinase 5 Phosphorylation of Collapsin Response Mediator Protein 1

et al. 2007

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Collapsin response mediator protein 1 (CRMP1) is one of the CRMP family members that mediates signal transduction of axonal guidance and neuronal migration. We show here evidence that CRMP1 is involved in semaphorin3A (Sema3A)-induced spine development in the cerebral cortex. In the cultured cortical neurons from crmp1 ϩ/Ϫ mice, Sema3A increased the density of clusters of synapsin I and postsynaptic density-95, but this increase was markedly attenuated in crmp1 Ϫ/Ϫ mice. This attenuation was also seen in cyclin-dependent kinase 5 (cdk5) Ϫ/Ϫ neurons. Furthermore, the introduction of wild-type CRMP1 but not CRMP1-T509A/S522A, (Thr 509 and Ser 522 were replaced by Ala), a mutant that cannot be phosphorylated by Cdk5, into crmp1 Ϫ/Ϫ neurons rescued the defect in Sema3A responsiveness. The Golgi-impregnation method showed that the crmp1 Ϫ/Ϫ layer V cortical neurons showed a lower density of synaptic bouton-like structures and that this phenotype had genetic interaction with sema3A. These findings suggest that Sema3A-induced spine development is regulated by phosphorylation of CRMP1 by Cdk5.

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Correlation between Semaphorin3A-Induced Facilitation of Axonal Transport and Local Activation of a Translation Initiation Factor Eukaryotic Translation Initiation Factor 4E

Cited by 64 publications

References 44 publications

Semaphorin3A Signaling Mediated by Fyn-dependent Tyrosine Phosphorylation of Collapsin Response Mediator Protein 2 at Tyrosine 32

Semaphorin3A Signaling Mediated by Fyn-dependent Tyrosine Phosphorylation of Collapsin Response Mediator Protein 2 at Tyrosine 32

The Role of Protein Synthesis in Striatal Long-Term Depression

Regulation of Spine Development by Semaphorin3A through Cyclin-Dependent Kinase 5 Phosphorylation of Collapsin Response Mediator Protein 1

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