ErbB1 receptor ligands attenuate the expression of synaptic scaffolding proteins, GRIP1 and SAP97, in developing neocortex

Yokomaku, Daisaku; Jourdi, Hussam; Kakita, Akiyoshi; Nagano, Tadasato; Takahashi, Hitoshi; Takei, Nobuyuki; Nawa, Hiroyuki

doi:10.1016/j.neuroscience.2005.08.014

Cited by 17 publications

(15 citation statements)

References 46 publications

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“…4L, M). GRIP1 has been previously implicated in modulating EGFR function in human cells (Yokomaku et al, 2005), and our findings extend these observations to KIF5B-RET.…”

Section: Resultssupporting

confidence: 88%

KIF5B-RET Oncoprotein Signals through a Multi-kinase Signaling Hub

Das

Cagan

2017

Cell Reports

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Summary Gene fusions are increasingly recognized as important cancer drivers. KIF5B-RET gene was recently identified as a primary driver in a subset of lung adenocarcinomas. Targeting human KIF5B-RET to epithelia in Drosophila directed multiple aspects of transformation including hyperproliferation, epithelial-to-mesenchymal transition, invasion, and extension of striking invadopodia-like processes. KIF5B-RET-transformed human bronchial cell line showed similar aspects of transformation including invadopodia-like processes. Through a combination of genetic and biochemical studies we demonstrate that the kinesin and kinase domains of KIF5B-RET act together to establish an emergent microtubule and RAB vesicle-dependent RET-SRC-EGFR-FGFR ‘signaling hub’. We demonstrate that drugs designed to inhibit RET alone work poorly in KIF5B-RET-transformed cells. However, combining the RET inhibitor sorafenib with drugs that target EGFR or microtubules or FGFR led to strong efficacy in both Drosophila and human cell line KIF5B-RET models. This work demonstrates the utility in exploring the full biology of fusions to identify rational therapeutic strategies.

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“…4L, M). GRIP1 has been previously implicated in modulating EGFR function in human cells (Yokomaku et al, 2005), and our findings extend these observations to KIF5B-RET.…”

Section: Resultssupporting

confidence: 88%

KIF5B-RET Oncoprotein Signals through a Multi-kinase Signaling Hub

Das

Cagan

2017

Cell Reports

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“…BDNF treatment upregulates the expression of AMPAr subunits and their associated PDZ proteins (AMPAr compartment) and enables synaptic plasticity associated with AMPAr subunits and their scaffolding proteins in various types of neurons but has little or no effects on NMDA receptors [25]–[27], [31], [32], [39]–[42]. Other trophic factors and cytokines including bFGF, EGF, and TGFα exert effects opposite to those of BDNF on AMPAr subunits and their associated scaffolding proteins [34], [43], [44]. AMPAr subunit stabilization at synapses is critical for the maintenance of long term encoding of synaptic events, such as those involved in late phase long term potentiation (l-LTP) and persistence of memory [14], [15], [45]–[47].…”

Section: Discussionmentioning

confidence: 99%

Acute BDNF Treatment Upregulates GluR1-SAP97 and GluR2-GRIP1 Interactions: Implications for Sustained AMPA Receptor Expression

Jourdi

Kabbaj

2013

PLoS ONE

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Brain-derived neurotrophic factor (BDNF) plays several prominent roles in synaptic plasticity and in learning and memory formation. Reduced BDNF levels and altered BDNF signaling have been reported in several brain diseases and behavioral disorders, which also exhibit reduced levels of AMPAr subunits. BDNF treatment acutely regulates AMPA receptor expression and function, including synaptic AMPAr subunit trafficking, and implicates several well defined signaling molecules that are required to elicit long term potentiation and depression (LTP and LTD, respectively). Long term encoding of synaptic events, as in long term memory formation, requires AMPAr stabilization and maintenance. However, factors regulating AMPAr stabilization in neuronal cell membranes and synaptic sites are not well characterized. In this study, we examine the effects of acute BDNF treatment on levels of AMPAr-associated scaffolding proteins and on AMPAr subunit-scaffolding protein interactions. We also examine the effects of BDNF-dependent enhanced interactions between AMPAr subunits with their specific scaffolding proteins on the accumulation of both types of proteins. Our results show that acute BDNF treatment upregulates the interactions between AMPAr subunits (GluR1 and GluR2) with their scaffold proteins SAP97 and GRIP1, respectively, leading to prolonged increased accumulation of both categories of proteins, albeit with distinct mechanisms for GluR1 and GluR2. Our findings reveal a new role for BDNF in the long term maintenance of AMPA receptor subunits and associated scaffolding proteins at synapses and further support the role of BDNF as a key regulator of synaptic consolidation. These results have potential implications for recent findings implicating BDNF and AMPAr subunits in various brain diseases and behavioral disorders.

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“…In addition, BDNF effects on AMPA receptors involve the activation of Nethylmaleimide-sensitive factor (NSF) and the subsequent recruitment of the AMPA receptor-associated PDZ scaffolding molecules (Narisawa-Saito et al, 2002;Jourdi et al, 2003). Our recent results indicate that EGF and other ErbB1 ligands down-regulates the expression of the AMPA receptor-associating PDZ molecules such as SAP-97 and GRIP, which bind to AMPA receptors and stabilize them by providing a link to cytoskeleton of postsynaptic sites (Yokomaku et al, 2005). Therefore, it is possible that BDNF and TGFα also contribute to postsynaptic organization of the AMPA receptors by positively and negatively influencing the expression of PDZ scaffolding proteins as well.…”

Section: Competition Between the Positive And Negative Regulators Bdmentioning

confidence: 97%

“…Although these factors are known to stimulate proliferation of progenitor and glial cells (Rabchevsky et al, 1998;Kornblum et al, 1999), the ErbB1 ligands had no effects on an astrocyte marker, glial fibrillary acidic protein (GFAP), and total protein recovery per dish under the given culture condition (see Experimental methods). The use of serum-free growth medium suppressed cell proliferation and reduced glial proportion to enable us to evaluate TGFα effects on cultured neurons (Yokomaku et al, 2005). As almost all ErbB1 ligands had the same impact on AMPA receptor expression, we focused on TGFα and analyzed its effects on AMPAtype glutamate receptor function.…”

Section: Subchronic Effects Of Erbb1 Ligands On Ampa-type Glutamate Rmentioning

confidence: 99%

“…It is possible that the observed alteration in the affinity of AMPA binding might be caused by posttranslational modification of AMPA receptors following ErbB1 activation (Matsuda et al, 1999;Suzuki et al, 2005). Alternatively, the ErbB1 activation reduces the expression of AMPA receptor-associating PDZ proteins, SAP97 and GRIP1, and potentially influences subcellular distributions and affinity of the AMPA receptor subunits (Yokomaku et al, 2005). The real nature of the affinity increase awaits further investigation at molecular levels.…”

Section: Distinction Between Mitotic Activity and Ampa Receptor-reducmentioning

confidence: 99%

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Transforming growth factor alpha attenuates the functional expression of AMPA receptors in cortical GABAergic neurons

Namba

Nagano

Iwakura

et al. 2006

Molecular and Cellular Neuroscience

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In the developing neocortex, brain-derived neurotrophic factor (BDNF) exerts a trophic activity to increase the expression and channel activity of α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA)-type glutamate receptor subunits. Here, we demonstrate that the epidermal growth factor (EGF) receptor (ErbB1) ligands exert the opposite biological activity in cultured neocortical neurons. Subchronic stimulation of ErbB1 with transforming growth factor α (TGFα), EGF, or heparin-binding EGF (HB-EGF) down-regulated protein expression of the GluR1 AMPA receptor subunit in cultured neocortical neurons. In agreement, TGFα treatment decreased the B max of [ 3 H] AMPA binding and GluR1 mRNA levels. Immunocytochemistry revealed that the decrease in GluR1 was most pronounced in multipolar GABAergic neurons. To examine the physiological consequences, we recorded AMPA-evoked currents as well as miniature excitatory postsynaptic currents in morphologically identified putative GABAergic neurons in culture. Subchronic TGFα treatment decreased AMPA-triggered currents as well as the amplitude and frequency of miniature excitatory postsynaptic currents. An ErbB1 tyrosine kinase inhibitor, PD153035, inhibited the TGFα effect. Moreover, TGFα counteracted the neurotrophic activity of BDNF on AMPA receptor expression. Co-application of TGFα with BDNF blocked the BDNF-triggered up-regulation of AMPA receptor expression and currents. These observations reveal a negative regulatory activity of the ErbB1 ligand, TGFα, which reduces the input sensitivity of cortical GABAergic neurons to attenuate their inhibitory function.

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ErbB1 receptor ligands attenuate the expression of synaptic scaffolding proteins, GRIP1 and SAP97, in developing neocortex

Cited by 17 publications

References 46 publications

KIF5B-RET Oncoprotein Signals through a Multi-kinase Signaling Hub

KIF5B-RET Oncoprotein Signals through a Multi-kinase Signaling Hub

Acute BDNF Treatment Upregulates GluR1-SAP97 and GluR2-GRIP1 Interactions: Implications for Sustained AMPA Receptor Expression

Transforming growth factor alpha attenuates the functional expression of AMPA receptors in cortical GABAergic neurons

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