Evidence map›Paper›PMID 21723917›Full record

ReviewBiochimica et biophysica acta2011

Mannose 6-phosphate receptor homology (MRH) domain-containing lectins in the secretory pathway.

Alicia C Castonguay, Linda J Olson, Nancy M Dahms

Abstract readReview
In one paragraph

Review in Biochimica et biophysica acta, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.4field-weighted citation impact, top 20% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

17 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. N-Glycosylation.Advances in experimental medicine and biology · 2021
    Article
  5. Review
  6. Article
  7. Article
  8. Biological roles of glycans.Glycobiology · 2017
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Review
  15. Article
  16. Insulin in the brain: there and back again.Pharmacology & therapeutics · 2012
    Review
  17. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Alicia C CastonguayDepartment of Biochemistry, Medical College of Wisconsin, Milwaukee, WI 53226, USA.
Linda J Olson
Nancy M Dahms
Medical College of Wisconsin · US

Funding

STRUCTURAL ANALYSIS OF THE MANNOSE 6-PHOSPHATE RECEPTORSR01DK042667 · NIDDK · MEDICAL COLLEGE OF WISCONSIN · PI DAHMS, NANCY M. · 1997 to 2023
$9.8M
NIDDK NIH HHS R01 DK042667
6 · The paper itself

Abstract

backgroundThe mannose 6-phosphate receptor homology (MRH) domain-containing family of proteins, which include recycling receptors (mannose 6-phosphate receptors, MPRs), resident endoplasmic reticulum (ER) proteins (glucosidase II β-subunit, XTP3-B, OS-9), and a Golgi glycosyltransferase (GlcNAc-phosphotransferase γ-subunit), are characterized by the presence of one or more MRH domains. Many MRH domains act as lectins and bind specific phosphorylated (MPRs) or non-phosphorylated (glucosidase II β-subunit, XTP3-B and OS-9) high mannose-type N-glycans. The MPRs are the only proteins known to bind mannose 6-phosphate (Man-6-P) residues via their MRH domains. SCOPE OF REVIEW: Recent biochemical and structural studies that have provided valuable insight into the glycan specificity and mechanisms of carbohydrate recognition by this diverse group of MRH domain-containing proteins are highlighted. MAJOR

conclusionsCurrently, three-dimensional structures are known for ten MRH domains, revealing the conservation of a similar fold. OS-9 and the MPRs use the same four residues (Gln, Arg, Glu, and Tyr) to bind mannose. GENERAL SIGNIFICANCE: The MRH domain-containing proteins play key roles in the secretory pathway: glucosidase II, XTP3-B, and OS-9 are involved in the recognition of nascent glycoproteins, whereas the MPRs play an essential role in lysosome biogenesis by targeting Man-6-P-containing lysosomal enzymes to the lysosome.

Indexed as

Amino Acid SequenceAnimalsHumansLectinsLysosomesMannosephosphatesModels, MolecularNeoplasm ProteinsPolysaccharidesProtein Structure, TertiaryReceptor, IGF Type 2Secretory PathwaySequence AlignmentSubstrate SpecificityLectinsmannose-6-phosphateMannosephosphatesNeoplasm ProteinsOS9 protein, humanPolysaccharidesReceptor, IGF Type 2

Identifiers

PMID21723917
PMCPMC3150748
OpenAlexW1975899889

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

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.