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Giantin antibody


Antibody ID


Target Antigen

Giantin antibody human, mouse, rat, hamster, monkey, non-human primate, hamster, human, mouse, rat

Proper Citation

(Abcam Cat# ab24586, RRID:AB_448163)


polyclonal antibody


validation status unknown, seller recommendations provided in 2012: Immunohistochemistry; Immunofluorescence; Immunocytochemistry; Western Blot; Immunohistochemistry - frozen; ICC/IF, IHC (PFA fixed), IHC-Fr, WB

Host Organism




Cat Num


APC Inhibits Ligand-Independent Wnt Signaling by the Clathrin Endocytic Pathway.

  • Saito-Diaz K
  • Dev. Cell
  • 2018 Mar 12

Literature context:


Adenomatous polyposis coli (APC) mutations cause Wnt pathway activation in human cancers. Current models for APC action emphasize its role in promoting β-catenin degradation downstream of Wnt receptors. Unexpectedly, we find that blocking Wnt receptor activity in APC-deficient cells inhibits Wnt signaling independently of Wnt ligand. We also show that inducible loss of APC is rapidly followed by Wnt receptor activation and increased β-catenin levels. In contrast, APC2 loss does not promote receptor activation. We show that APC exists in a complex with clathrin and that Wnt pathway activation in APC-deficient cells requires clathrin-mediated endocytosis. Finally, we demonstrate conservation of this mechanism in Drosophila intestinal stem cells. We propose a model in which APC and APC2 function to promote β-catenin degradation, and APC also acts as a molecular "gatekeeper" to block receptor activation via the clathrin pathway.

Funding information:
  • BLRD VA - I01 BX001426()
  • NCATS NIH HHS - UL1 TR000445()
  • NCATS NIH HHS - UL1 TR002243()
  • NCI NIH HHS - P30 CA068485()
  • NCI NIH HHS - P50 CA095103()
  • NCI NIH HHS - R01 CA069457()
  • NCI NIH HHS - R01 CA105038()
  • NIDDK NIH HHS - F30 DK111107()
  • NIDDK NIH HHS - R01 DK099204()
  • NIGMS NIH HHS - R01 GM081635()
  • NIGMS NIH HHS - R01 GM103926()
  • NIGMS NIH HHS - R01 GM106720()
  • NIGMS NIH HHS - R01 GM121421()
  • NIGMS NIH HHS - R01 GM122222()
  • NIGMS NIH HHS - R35 GM122516()
  • NIGMS NIH HHS - T32 GM007347()
  • NIH HHS - OD008466(United States)
  • NIH HHS - P40 OD018537()

In Situ Architecture and Cellular Interactions of PolyQ Inclusions.

  • Bäuerlein FJB
  • Cell
  • 2017 Sep 21

Literature context:


Expression of many disease-related aggregation-prone proteins results in cytotoxicity and the formation of large intracellular inclusion bodies. To gain insight into the role of inclusions in pathology and the in situ structure of protein aggregates inside cells, we employ advanced cryo-electron tomography methods to analyze the structure of inclusions formed by polyglutamine (polyQ)-expanded huntingtin exon 1 within their intact cellular context. In primary mouse neurons and immortalized human cells, polyQ inclusions consist of amyloid-like fibrils that interact with cellular endomembranes, particularly of the endoplasmic reticulum (ER). Interactions with these fibrils lead to membrane deformation, the local impairment of ER organization, and profound alterations in ER membrane dynamics at the inclusion periphery. These results suggest that aberrant interactions between fibrils and endomembranes contribute to the deleterious cellular effects of protein aggregation. VIDEO ABSTRACT.

Efficient protein targeting to the inner nuclear membrane requires Atlastin-dependent maintenance of ER topology.

  • Pawar S
  • Elife
  • 2017 Aug 14

Literature context:


Newly synthesized membrane proteins are targeted to the inner nuclear membrane (INM) by diffusion within the membrane system of the endoplasmic reticulum (ER), translocation through nuclear pore complexes (NPCs) and retention on nuclear partners. Using a visual in vitro assay we previously showed that efficient protein targeting to the INM depends on nucleotide hydrolysis. We now reveal that INM targeting is GTP-dependent. Exploiting in vitro reconstitution and in vivo analysis of INM targeting, we establish that Atlastins, membrane-bound GTPases of the ER, sustain the efficient targeting of proteins to the INM by their continued activity in preserving ER topology. When ER topology is altered, the long-range diffusional exchange of proteins in the ER network and targeting efficiency to the INM are diminished. Highlighting the general importance of proper ER topology, we show that Atlastins also influence NPC biogenesis and timely exit of secretory cargo from the ER.

The Golgi apparatus acts as a platform for TBK1 activation after viral RNA sensing.

  • Pourcelot M
  • BMC Biol.
  • 2016 Aug 18

Literature context:


BACKGROUND: After viral infection and the stimulation of some pattern-recognition receptors, TANK-binding kinase I (TBK1) is activated by K63-linked polyubiquitination followed by trans-autophosphorylation. While the activated TBK1 induces type I interferon production by phosphorylating the transcription factor IRF3, the precise molecular mechanisms underlying TBK1 activation remain unclear. RESULTS: We report here the localization of the ubiquitinated and phosphorylated active form of TBK1 to the Golgi apparatus after the stimulation of RIG-I-like receptors (RLRs) or Toll-like receptor-3 (TLR3), due to TBK1 K63-linked ubiquitination on lysine residues 30 and 401. The ubiquitin-binding protein optineurin (OPTN) recruits ubiquitinated TBK1 to the Golgi apparatus, leading to the formation of complexes in which TBK1 is activated by trans-autophosphorylation. Indeed, OPTN deficiency in various cell lines and primary cells impairs TBK1 targeting to the Golgi apparatus and its activation following RLR or TLR3 stimulation. Interestingly, the Bluetongue virus NS3 protein binds OPTN at the Golgi apparatus, neutralizing its activity and thereby decreasing TBK1 activation and downstream signaling. CONCLUSIONS: Our results highlight an unexpected role of the Golgi apparatus in innate immunity as a key subcellular gateway for TBK1 activation after RNA virus infection.

Funding information:
  • NICHD NIH HHS - NIH P30 HD003352(United States)
  • NIGMS NIH HHS - T32 GM007184(United States)

PAT1 inversely regulates the surface Amyloid Precursor Protein level in mouse primary neurons.

  • Dilsizoglu Senol A
  • BMC Neurosci
  • 2015 Mar 7

Literature context:


BACKGROUND: The amyloid precursor protein (APP) is a key molecule in Alzheimer disease. Its localization at the cell surface can trigger downstream signaling and APP cleavages. APP trafficking to the cell surface in neurons is not clearly understood and may be related to the interactions with its partners. In this respect, by having homologies with kinesin light chain domains and because of its capacity to bind APP, PAT1 represents a good candidate. RESULTS: We observed that PAT1 binds poorly APP at the cell surface of primary cortical neurons contrary to cytoplasmic APP. Using down and up-regulation of PAT1, we observed respectively an increase and decrease of APP at the cell surface. The increase of APP at the cell surface induced by low levels of PAT1 did not trigger cell death signaling. CONCLUSIONS: These data suggest that PAT1 slows down APP trafficking to the cell surface in primary cortical neurons. Our results contribute to the elucidation of mechanisms involved in APP trafficking in Alzheimer disease.

Funding information:
  • NEI NIH HHS - 5-T32EY013360-13(United States)
  • NIDCD NIH HHS - F32 DC000210(United States)