Evidence map›Paper›PMID 21570947›Full record

ArticleBiochimica et biophysica acta2011

Role of the putative N-glycosylation and PKC-phosphorylation sites of the human sodium-dependent multivitamin transporter (hSMVT) in function and regulation.

Abhisek Ghosal, Veedamali S Subramanian, Hamid M Said

Abstract read
In one paragraph

Article 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 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.8field-weighted citation impact, top 16% 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

16 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Tamoxifen-induced, intestinal-specific deletion ofAmerican journal of physiology. Gastrointestinal and liver physiology · 2019
    Article
  7. Article
  8. Structure/functional aspects of the human riboflavin transporter-3 (American journal of physiology. Cell physiology · 2017
    Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
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  15. Review
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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.

Abhisek GhosalDepartment of Medicine and Physiology/Biophysics, University of California, Irvine, CA 92697, USA.
Veedamali S Subramanian
Hamid M Said
University of California, Irvine · US

Funding

INTESTINAL VITAMIN H UPTAKE--MOLECULAR/CELL REGULATIONR01DK058057 · NIDDK · UNIVERSITY OF CALIFORNIA-IRVINE · PI SAID, HAMID M · 2000 to 2019
$6.8M
Vitamin B1 (thiamin) transport in Alzheimer’s Disease: Role of microRNAs in regulating level of expression of its transporters (SLC19A2 & SLC19A3) in human brain cells and effect of hypoxiaR01DK056061 · NIDDK · UNIVERSITY OF CALIFORNIA-IRVINE · PI SAID, HAMID M · 1999 to 2024
$5.0M
Mechanism/Regulation of Intestinal Thiamin UptakeR37DK056061 · NIDDK · UNIVERSITY OF CALIFORNIA-IRVINE · PI SAID, HAMID M · 2009 to 2018
$3.6M
NIDDK NIH HHS DK56061NIDDK NIH HHS DK58057NIDDK NIH HHS R01 DK056061NIDDK NIH HHS R01 DK058057NIDDK NIH HHS R37 DK056061
6 · The paper itself

Abstract

The sodium-dependent multivitamin transporter (SMVT) is a major biotin transporter in a variety of tissues including the small intestine. The human SMVT (hSMVT) polypeptide is predicted to have four N-glycosylation sites and two putative PKC phosphorylation sites but their role in the function and regulation of the protein is not known and was examined in this investigation. Our results showed that the hSMVT protein is glycosylated and that this glycosylation is important for its function. Studies utilizing site-directed mutagenesis revealed that the N-glycosylation sites at positions Asn(138) and Asn(489) are important for the function of hSMVT and that mutating these sites significantly reduces the V(max) of the biotin uptake process. Mutating the putative PKC phosphorylation site Thr(286) of hSMVT led to a significant decrease in the PMA-induced inhibition in biotin uptake. The latter effect was not mediated via changes in the level of expression of the hSMVT protein and mRNA or in its level of expression at the cell membrane. These findings demonstrate that the hSMVT protein is glycosylated, and that glycosylation is important for its function. Furthermore, the study shows a role for the putative PKC-phosphorylation site Thr(286) of hSMVT in the PKC-mediated regulation of biotin uptake.

Indexed as

Protein Processing, Post-TranslationalAsparagineBiological TransportBiotinCaco-2 CellsGlycosylationHumansMutagenesis, Site-DirectedMutationPhosphorylationProtein ConformationProtein Kinase CRetinal Pigment EpitheliumStructure-Activity RelationshipSymportersTetradecanoylphorbol AcetateAsparagineBiotinbiotin transporterProtein Kinase CSymportersTetradecanoylphorbol AcetateThreonineTunicamycin

Identifiers

PMID21570947
PMCPMC3130002
OpenAlexW2072028447

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.