Chaparral Labs
back to search

protein

Atlastin-2

aka ATL-2

ATL2
protein:Q8NHH9disease:adad:direction:down

Gene

ATL2

Organism

Homo sapiens(9606)

Length

583 aa

Mass

66,229 Da

AI summarysource-grounded · cited inline
claude-haiku-4-5-20251001

Atlastin-2 (ATL2) is a membrane-anchored GTPase that mediates GTP-dependent fusion of endoplasmic reticulum (ER) membranes, maintaining the structural integrity of the continuous ER network (UniProt: Q8NHH9). The protein facilitates formation of three-way ER tubule junctions by forming homodimers through its G domains; upon GTP hydrolysis, conformational changes tighten the dimer and pull adjacent membranes together to drive fusion, after which the homodimer disassembles and resets for subsequent fusion cycles.

ATL2 is widely expressed and functions in fundamental ER homeostasis and morphology. No disease associations are documented in UniProt for this protein.

ATL2 shows down-regulation in Alzheimer's Disease brain tissue. Chaparral AD proteomics analysis of post-mortem human AD brain versus age-matched controls identified ATL2 as decreased (mean log2 fold-change: −0.41) in TMT-labeled quantitative proteomics across subcellular fractions (P2, P3, S2, S3). This reduction may reflect compromised ER membrane dynamics and network integrity in the AD pathological state.

Generated from the curated entity record below. May contain errors — verify against source links.

Proteomics Evidence · AD

↓ Down in AD

P3

not detected

P2

not detected

S2

not detected

S3

-0.411

Mean log₂FC across detected fractions: -0.4112 (1 of 4 fractions detected)

Human post-mortem AD brain vs age-matched controls, TMT-labeled, 4 subcellular fractions (P2, P3, S2, S3), DDA proteomics.

Related Publications

Browse all →

Function

Atlastin-2 (ATL2) is a membrane-anchored GTPase that mediates the GTP-dependent fusion of endoplasmic reticulum (ER) membranes, maintaining the continuous ER network. It facilitates the formation of three-way junctions where ER tubules intersect (PubMed:18270207, PubMed:19665976, PubMed:22065636, PubMed:27619977, PubMed:34817557). Two atlastin-2 on neighboring ER tubules bind GTP and form loose homodimers through the GB1/RHD3-type G domains and 3HB regions. Upon GTP hydrolysis, the 3HB regions tighten, pulling the membranes together to drive their fusion. After fusion, the homodimer disassembles upon release of inorganic phosphate (Pi). Subsequently, GDP dissociates, resetting the monomers to a conformation ready for a new fusion cycle (By similarity)

Sources

Last updated 5/8/2026, 6:28:28 AM