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PMID |
Sentence |
1 |
19794150
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Here we show that Slo1 proteins interact with Neph1, a member of the immunoglobulin superfamily expressed in slit diaphragm domains of podocytes and in vertebrate and invertebrate nervous systems.
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2 |
19794150
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Neph1 can interact with all three extreme COOH-terminal variants of Slo1 (Slo1(VEDEC), Slo1(QEERL), and Slo1(EMVYR)) as ascertained by glutathione S-transferase (GST) pull-down assays and by coimmunoprecipitation.
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3 |
19794150
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Neph1 is partially colocalized in intracellular compartments with endogenous Slo1 in podocytes and ciliary ganglion neurons.
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4 |
19794150
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Consistent with this, small interfering RNA (siRNA) knockdown of endogenous Neph1 in embryonic day 10 ciliary ganglion neurons causes an increase in steady-state surface expression of Slo1 and an increase in whole cell Ca(2+)-dependent K(+) current.
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5 |
19794150
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Surprisingly, a comparable Neph1 knockdown in podocytes causes a decrease in surface expression of Slo1 and a decrease in whole cell BK(Ca) currents.
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6 |
19794150
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In podocytes, Neph1 siRNA also caused a decrease in nephrin, even though the Neph1 siRNA had no sequence homology with nephrin.
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7 |
21402783
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Unlike wild-type Myo1c, the membrane localization of Neph1 was significantly reduced in podocytes expressing dominant negative Myo1c.
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8 |
21402783
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We further demonstrate that similarly to Neph1, Myo1c also binds nephrin and reduces its localization at the podocyte cell membrane.
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9 |
18258597
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Furthermore, Neph1 attenuates ERK activation elicited by Fyn, and this inhibitory effect requires the intact binding motif for the Grb2 SH2 domain.
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10 |
18258597
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Our results shown here demonstrate that Neph1 is a novel in vivo substrate of SFK and suggest that Neph1 modulates ERK signaling through phosphorylation-dependent interaction with Grb2.
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