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c-Myc (9E11) antibody

RRID:AB_627266

Antibody ID

AB_627266

Target Antigen

c-Myc (9E11) mouse, human, monkey, mouse, human, non-human primate

Vendor

Santa Cruz Biotechnology

Cat Num

sc-47694

Proper Citation

(Santa Cruz Biotechnology Cat# sc-47694, RRID:AB_627266)

Clonality

monoclonal antibody

Host Organism

mouse

Comments

validation status unknown check with seller; recommendations: WB, IP, IF, IHC(P); Immunofluorescence; Immunohistochemistry; Western Blot; Immunocytochemistry; Immunoprecipitation

Publications that use this research resource

Myotubularin related protein-2 and its phospholipid substrate PIP2 control Piezo2-mediated mechanotransduction in peripheral sensory neurons.

  • Narayanan P
  • Elife
  • 2018 Mar 9

Literature context: 0, 1:500) Santa Cruz, #sc-47694 RRID:AB_627266


Abstract:

Piezo2 ion channels are critical determinants of the sense of light touch in vertebrates. Yet, their regulation is only incompletely understood. We recently identified myotubularin related protein-2 (Mtmr2), a phosphoinositide (PI) phosphatase, in the native Piezo2 interactome of murine dorsal root ganglia (DRG). Here, we demonstrate that Mtmr2 attenuates Piezo2-mediated rapidly adapting mechanically activated (RA-MA) currents. Interestingly, heterologous Piezo1 and other known MA current subtypes in DRG appeared largely unaffected by Mtmr2. Experiments with catalytically inactive Mtmr2, pharmacological blockers of PI(3,5)P2 synthesis, and osmotic stress suggest that Mtmr2-dependent Piezo2 inhibition involves depletion of PI(3,5)P2. Further, we identified a PI(3,5)P2 binding region in Piezo2, but not Piezo1, that confers sensitivity to Mtmr2 as indicated by functional analysis of a domain-swapped Piezo2 mutant. Altogether, our results propose local PI(3,5)P2 modulation via Mtmr2 in the vicinity of Piezo2 as a novel mechanism to dynamically control Piezo2-dependent mechanotransduction in peripheral sensory neurons.

Funding information:
  • Deutsche Forschungsgemeinschaft - CRC 937 Project A13()
  • Deutsche Forschungsgemeinschaft - CRC889 Project A9()
  • Deutsche Forschungsgemeinschaft - GO 2481/2-1()
  • Deutsche Forschungsgemeinschaft - SCHM 2533/2-1()
  • Göttinger Graduiertenschule für Neurowissenschaften, Biophysik und Molekulare Biowissenschaften - PhD fellowship()
  • Max-Planck-Gesellschaft - Open-access funding()
  • NIMH NIH HHS - R37 MH059520(United States)

Cadherin-10 Maintains Excitatory/Inhibitory Ratio through Interactions with Synaptic Proteins.

  • Smith KR
  • J. Neurosci.
  • 2017 Nov 15

Literature context: sity of Iowa Hybridoma Bank and RRID:AB_627266; Santa Cruz Biotechnology), rab


Abstract:

Appropriate excitatory/inhibitory (E/I) balance is essential for normal cortical function and is altered in some psychiatric disorders, including autism spectrum disorders (ASDs). Cell-autonomous molecular mechanisms that control the balance of excitatory and inhibitory synapse function remain poorly understood; no proteins that regulate excitatory and inhibitory synapse strength in a coordinated reciprocal manner have been identified. Using super-resolution imaging, electrophysiology, and molecular manipulations, we show that cadherin-10, encoded by CDH10 within the ASD risk locus 5p14.1, maintains both excitatory and inhibitory synaptic scaffold structure in cultured cortical neurons from rats of both sexes. Cadherin-10 localizes to both excitatory and inhibitory synapses in neocortex, where it is organized into nanoscale puncta that influence the size of their associated PSDs. Knockdown of cadherin-10 reduces excitatory but increases inhibitory synapse size and strength, altering the E/I ratio in cortical neurons. Furthermore, cadherin-10 exhibits differential participation in complexes with PSD-95 and gephyrin, which may underlie its role in maintaining the E/I ratio. Our data provide a new mechanism whereby a protein encoded by a common ASD risk factor controls E/I ratios by regulating excitatory and inhibitory synapses in opposing directions.SIGNIFICANCE STATEMENT The correct balance between excitatory/inhibitory (E/I) is crucial for normal brain function and is altered in psychiatric disorders such as autism. However, the molecular mechanisms that underlie this balance remain elusive. To address this, we studied cadherin-10, an adhesion protein that is genetically linked to autism and understudied at the cellular level. Using a combination of advanced microscopy techniques and electrophysiology, we show that cadherin-10 forms nanoscale puncta at excitatory and inhibitory synapses, maintains excitatory and inhibitory synaptic structure, and is essential for maintaining the correct balance between excitation and inhibition in neuronal dendrites. These findings reveal a new mechanism by which E/I balance is controlled in neurons and may bear relevance to synaptic dysfunction in autism.

Metaphase chromosome structure is dynamically maintained by condensin I-directed DNA (de)catenation.

  • Piskadlo E
  • Elife
  • 2017 May 6

Literature context: sc-47694 RRID:AB_627266), anti-α-t


Abstract:

Mitotic chromosome assembly remains a big mystery in biology. Condensin complexes are pivotal for chromosome architecture yet how they shape mitotic chromatin remains unknown. Using acute inactivation approaches and live-cell imaging in Drosophila embryos, we dissect the role of condensin I in the maintenance of mitotic chromosome structure with unprecedented temporal resolution. Removal of condensin I from pre-established chromosomes results in rapid disassembly of centromeric regions while most chromatin mass undergoes hyper-compaction. This is accompanied by drastic changes in the degree of sister chromatid intertwines. While wild-type metaphase chromosomes display residual levels of catenations, upon timely removal of condensin I, chromosomes present high levels of de novo Topoisomerase II (TopoII)-dependent re-entanglements, and complete failure in chromosome segregation. TopoII is thus capable of re-intertwining previously separated DNA molecules and condensin I continuously required to counteract this erroneous activity. We propose that maintenance of chromosome resolution is a highly dynamic bidirectional process.