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alpha Tubulin Antibody

RRID:AB_521686

Antibody ID

AB_521686

Target Antigen

alpha Tubulin chicken, bovine, guinea pig, human, xenopus, mouse, porcine, rat

Proper Citation

(Novus Cat# NB100-690, RRID:AB_521686)

Clonality

monoclonal antibody

Comments

Immunocytochemistry, Immunofluorescence, Immunohistochemistry-Paraffin, Immunoprecipitation, Western Blot

Clone ID

DM1A

Host Organism

mouse

Vendor

Novus

Cat Num

NB100-690

Publications that use this research resource

Remodeling of the Inner Hair Cell Microtubule Meshwork in a Mouse Model of Auditory Neuropathy AUNA1.

  • Surel C
  • eNeuro
  • 2017 Oct 24

Literature context:


Abstract:

Auditory neuropathy 1 (AUNA1) is a form of human deafness resulting from a point mutation in the 5' untranslated region of the Diaphanous homolog 3 (DIAPH3) gene. Notably, the DIAPH3 mutation leads to the overexpression of the DIAPH3 protein, a formin family member involved in cytoskeleton dynamics. Through study of diap3-overexpressing transgenic (Tg) mice, we examine in further detail the anatomical, functional, and molecular mechanisms underlying AUNA1. We identify diap3 as a component of the hair cells apical pole in wild-type mice. In the diap3-overexpressing Tg mice, which show a progressive threshold shift associated with a defect in inner hair cells (IHCs), the neurotransmitter release and potassium conductances are not affected. Strikingly, the overexpression of diap3 results in a selective and early-onset alteration of the IHC cuticular plate. Molecular dissection of the apical components revealed that the microtubule meshwork first undergoes aberrant targeting into the cuticular plate of Tg IHCs, followed by collapse of the stereociliary bundle, with eventual loss of the IHC capacity to transmit incoming auditory stimuli.

Funding information:
  • NIGMS NIH HHS - T32 GM007616(United States)

Nuclear pore assembly proceeds by an inside-out extrusion of the nuclear envelope.

  • Otsuka S
  • Elife
  • 2016 Sep 15

Literature context:


Abstract:

The nuclear pore complex (NPC) mediates nucleocytoplasmic transport through the nuclear envelope. How the NPC assembles into this double membrane boundary has remained enigmatic. Here, we captured temporally staged assembly intermediates by correlating live cell imaging with high-resolution electron tomography and super-resolution microscopy. Intermediates were dome-shaped evaginations of the inner nuclear membrane (INM), that grew in diameter and depth until they fused with the flat outer nuclear membrane. Live and super-resolved fluorescence microscopy revealed the molecular maturation of the intermediates, which initially contained the nuclear and cytoplasmic ring component Nup107, and only later the cytoplasmic filament component Nup358. EM particle averaging showed that the evagination base was surrounded by an 8-fold rotationally symmetric ring structure from the beginning and that a growing mushroom-shaped density was continuously associated with the deforming membrane. Quantitative structural analysis revealed that interphase NPC assembly proceeds by an asymmetric inside-out extrusion of the INM.

Funding information:
  • NINDS NIH HHS - NS051255(United States)