Evidence map›Paper›PMID 10908666›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2000

Recognition of the 300-kDa mannose 6-phosphate receptor cytoplasmic domain by 47-kDa tail-interacting protein.

J G Orsel, P M Sincock, J P Krise, S R Pfeffer

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.6field-weighted citation impact, top 11% 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

25 citing papers in PubMed, 67 citations in OpenAlex.

  1. Review
  2. Protein sorting from endosomes to the TGN.Frontiers in cell and developmental biology · 2023
    Review
  3. Review
  4. Review
  5. Article
  6. Review
  7. A role for retromer in hepatitis C virus replication.Cellular and molecular life sciences : CMLS · 2016
    Article
  8. Article
  9. Article
  10. Article
  11. Entry at the trans-face of the Golgi.Cold Spring Harbor perspectives in biology · 2011
    Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. Tail-interacting protein TIP47 is a connector between Gag and Env and is required for Env incorporation into HIV-1 virions.Proceedings of the National Academy of Sciences of the United States of America · 2006
    Article
  17. Article
  18. TIP47 is a key effector for Rab9 localization.The Journal of cell biology · 2006
    Article
  19. Article
  20. 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

4 authors at 1 institution in 1 country.

J G OrselDepartment of Biochemistry, Stanford University School of Medicine, Stanford, CA 94305-5307, USA.
P M Sincock
J P Krise
S R Pfeffer
Stanford University · US

Funding

NIDDK NIH HHS DK37336
6 · The paper itself

Abstract

Tail-interacting 47-kDa protein (TIP47) binds the cytoplasmic domains of the cation-dependent (CD) and cation-independent (CI) mannose 6-phosphate receptors (MPRs) and is required for their transport from endosomes to the Golgi complex. TIP47 recognizes a phenylalanine-tryptophan signal in the CD-MPR. We show here that TIP47 interaction with the 163-residue CI-MPR cytoplasmic domain is highly conformation dependent and requires CI-MPR residues that are proximal to the membrane. CI-MPR cytoplasmic domain residues 1-47 are dispensable, whereas residues 48-74 are essential for high-affinity binding. However, residues 48-74 are not sufficient for high-affinity binding; residues 75-163 alone display weak affinity for TIP47, yet they contribute to the presentation of residues 48-74 in the intact protein. Independent competition binding experiments confirm that TIP47 interacts with the membrane-proximal portion of the CI-MPR cytoplasmic domain. TIP47 binding is competed by the binding of the AP-2 clathrin adaptor at (and near) residues 24-29 but not by AP-1 binding at (and near) residues 160-161. Finally, TIP47 appears to recognize a putative loop generated by the sequence PPAPRPG and other hydrophobic residues in the membrane-proximal domain. Although crystallography will be needed to define the precise interaction interface, these data provide an initial structural basis for TIP47-CI-MPR association.

Indexed as

Intracellular Signaling Peptides and ProteinsPregnancy ProteinsAmino Acid SequenceBinding SitesCytoplasmDNA-Binding ProteinsPerilipin-3Protein BindingReceptor, IGF Type 2Recombinant Fusion ProteinsVesicular Transport ProteinsDNA-Binding ProteinsIntracellular Signaling Peptides and ProteinsPerilipin-3PLIN3 protein, humanPregnancy ProteinsReceptor, IGF Type 2Recombinant Fusion ProteinsVesicular Transport Proteins

Identifiers

PMID10908666
PMCPMC16819
OpenAlexW2051856959

What OpenQuestion holds

Textmetadata
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.