ArticleThe EMBO journal1998
A four-to-one association between peptide motifs: four C-terminal domains from cholinesterase assemble with one proline-rich attachment domain (PRAD) in the secretory pathway.
Article in The EMBO journal, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 83 citations in OpenAlex.
- Molecular Analysis of a Congenital Myasthenic Syndrome Due to a Pathogenic Variant Affecting the C-Terminus of ColQ.International journal of molecular sciences · 2023Article
- Neuroactive venom compounds obtained fromThe journal of venomous animals and toxins including tropical diseases · 2021Article
- Polyproline-rich peptides associated with Torpedo californica acetylcholinesterase tetramers.Chemico-biological interactions · 2020Article
- Cryo-EM structure of the native butyrylcholinesterase tetramer reveals a dimer of dimers stabilized by a superhelical assembly.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Hot Spots for Protein Partnerships at the Surface of Cholinesterases and Related α/β Hydrolase Fold Proteins or Domains-A Structural Perspective.Molecules (Basel, Switzerland) · 2017Review
- The C5 Variant of the Butyrylcholinesterase Tetramer Includes a Noncovalently Bound 60 kDa Lamellipodin Fragment.Molecules (Basel, Switzerland) · 2017Article
- Reassessment of the role of the central cholinergic system.Journal of molecular neuroscience : MN · 2014Review
- COOH-terminal collagen Q (COLQ) mutants causing human deficiency of endplate acetylcholinesterase impair the interaction of ColQ with proteins of the basal lamina.Human genetics · 2014Article
- Polyproline tetramer organizing peptides in fetal bovine serum acetylcholinesterase.Biochimica et biophysica acta · 2013Article
- Congenital hypothyroidism mutations affect common folding and trafficking in the α/β-hydrolase fold proteins.The FEBS journal · 2012Article
- Acetylcholinesterase: from 3D structure to function.Chemico-biological interactions · 2010Article
- Targeting acetylcholinesterase to membrane rafts: a function mediated by the proline-rich membrane anchor (PRiMA) in neurons.The Journal of biological chemistry · 2010Article
- Limiting role of protein disulfide isomerase in the expression of collagen-tailed acetylcholinesterase forms in muscle.The Journal of biological chemistry · 2009Article
- Targeting of acetylcholinesterase in neurons in vivo: a dual processing function for the proline-rich membrane anchor subunit and the attachment domain on the catalytic subunit.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2009Article
- Acetylcholinesterase expression in muscle is specifically controlled by a promoter-selective enhancesome in the first intron.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2008Article
- A tryptophan-rich motif in the carboxyl terminus of the small envelope protein of hepatitis B virus is central to the assembly of hepatitis delta virus particles.Journal of virology · 2006Article
- The association of tetrameric acetylcholinesterase with ColQ tail: a block normal mode analysis.PLoS computational biology · 2005Article
- LARGE SCALE PURIFICATION OF BUTYRYLCHOLINESTERASE FROM HUMAN PLASMA SUITABLE FOR INJECTION INTO MONKEYS; A POTENTIAL NEW THERAPEUTIC FOR PROTECTION AGAINST COCAINE AND NERVE AGENT TOXICITY.The journal of medical, chemical, biological, and radiological defense · 2005Article
- Tetrameric mouse acetylcholinesterase: continuum diffusion rate calculations by solving the steady-state Smoluchowski equation using finite element methods.Biophysical journal · 2005Article
- The synaptic acetylcholinesterase tetramer assembles around a polyproline II helix.The EMBO journal · 2004Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The major type of acetylcholinesterase in vertebrates (AChET) is characterized by the presence of a short C-terminal domain of 40 residues, the 'tryptophan amphiphilic tetramerization' (WAT) domain. The presence of this domain is not necessary for catalytic activity but is responsible for hydrophobic interactions and for the capacity of AChET subunits to form quaternary associations with anchoring proteins, thereby conditioning their functional localization. In the collagen tail of asymmetric forms, we characterized a small conserved region that is sufficient for binding an AChET tetramer, the proline-rich attachment domain (PRAD). We show that the WAT domain alone is sufficient for association with the PRAD, and that it can attach foreign proteins (alkaline phosphatase, GFP) to a PRAD-containing construct with a glycophosphatidylinositol anchor (GPI), and thus anchor them to the cell surface. Furthermore, we show that isolated WAT domains, or proteins containing a WAT domain, can replace individual AChET subunits in PRAD-linked tetramers. This suggests that the four WAT domains interact with the PRAD in a similar manner. These quaternary interactions can form without intercatenary disulfide bonds. The common catalytic domains of AChE are not necessary for tetrameric assembly, although they may contribute to the stability of the tetramer.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.