Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

ANKRD22 is an N-myristoylated hairpin-like monotopic membrane protein specifically localized to lipid droplets.

Scientific reports - 28 Sept 2021

Utsumi Toshihiko, Hosokawa Takuro, Shichita Mayu, Nishiue Misato, Iwamoto Natsuko, Harada Haruna, Kiwado Aya, Yano Manami, Otsuka Motoaki, Moriya Koko

Abstract excerpt

The membrane topology and intracellular localization of ANKRD22, a novel human N-myristoylated protein with a predicted single-pass transmembrane domain that was recently reported to be overexpressed in cancer, were examined. Immunofluorescence staining of COS-1 cells transfected with cDNA encoding ANKRD22 coupled with organelle markers revealed that ANKRD22 localized specifically to lipid droplets (LD). Analysis...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Cell-Free System
Share to Chlorocebus aethiops

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to COS Cells

Share to Insecta

Share to Lipid Droplets

Share to Membrane Proteins

Share to Myristic Acid

Share to Protein Processing, Post-Translational

Source

Open in PubMed Open full text

Identifiers

PMID: 34584137
DOI: 10.1038/s41598-021-98486-8
PMCID: PMC8478909

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

ANKRD22 is an N-myristoylated hairpin-like monotopic membrane protein specifically localized to lipid droplets.PMID 34584137Read ↗

The N-terminal intrinsically disordered region mediates intracellular localization and self-oligomerization of ALS2.Semantic proximity Read ↗

A proteome-wide screen for membrane-interactions in intrinsically disordered regions of transmembrane proteins reveals a role in diseaseSemantic proximity Read ↗

Comparative study of Dog and Human Lipid Droplet-associated protein (PLIN2)Semantic proximity Read ↗

UNC93B1 physically associates with human TLR8 and regulates TLR8-mediated signaling.Semantic proximity Read ↗

The palmitoylation state of PMP22 modulates epithelial cell morphology and migration.Semantic proximity Read ↗

Protein aggregation of SERCA2 mutants associated with Darier disease elicits ER stress and apoptosis in keratinocytes.Semantic proximity Read ↗

Substrate specificity, membrane topology, and activity regulation of human alkaline ceramidase 2 (ACER2).Semantic proximity Read ↗

Ankrd26 is critical for cell differentiation and cancer-linked mutations affect its key propertiesSemantic proximity Read ↗

Regulation of the Equilibrium between Closed and Open Conformations of Annexin A2 by N-Terminal Phosphorylation and S100A4-Binding.Semantic proximity Read ↗

Inhibition of ANKRD1 sensitizes human ovarian cancer cells to endoplasmic reticulum stress-induced apoptosisSemantic proximity Read ↗

Identification of a Regulatory Acidic Motif as the Determinant of Membrane Localization of TICAM-2.Semantic proximity Read ↗

AGR2 Gene Function Requires a Unique Endoplasmic Reticulum Localization MotifSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.