PMID- 10578063
OWN - NLM
STAT- MEDLINE
DCOM- 20000328
LR  - 20190513
IS  - 0021-924X (Print)
IS  - 0021-924X (Linking)
VI  - 126
IP  - 6
DP  - 1999 Dec
TI  - Indispensability of transmembrane domains of Golgi UDP-galactose transporter as
      revealed by analysis of genetic defects in UDP-galactose transporter-deficient
      murine had-1 mutant cell lines and construction of deletion mutants.
PG  - 1107-17
AB  - UDP-galactose transporter is a membrane protein localized in the Golgi apparatus.
      It translocates UDP-galactose from the cytosol into the Golgi lumen, thus
      providing galactosyltransferases with their substrate. We characterized murine
      UDP-galactose transporter through molecular cloning for the following purposes:
      (i) to elucidate the molecular bases underlying the genetic defects of murine
      Had-1 mutants, which are deficient in UDP-galactose transporting activity, and
      (ii) to obtain information that would help us in planning rational approaches to 
      identify functionally essential regions, based on comparison of primary
      structures between human and murine UDP-galactose transporters. We identified
      five nonsense mutations, one missense Gly178Asp mutation, and two aberrant
      splicing mutations. Although glycine178 is highly conserved among
      nucleotide-sugar transporters, a Gly178Ala variant was functional. The
      species-differences between human and murine UDP-galactose transporters were
      largely confined to the N- and C-terminal regions of the transporters.
      Substantial deletions in the N- and C-terminal regions did not lead to loss of
      UDP-galactose transporting activity, indicating that these cytosolic regions are 
      dispensable for the transporting activity. The transporter was fused with
      green-fluorescent protein at the C-terminal cytosolic tail without impairing the 
      functions of either protein. Our results demonstrate the importance of the
      transmembrane core region of the UDP-galactose transporter protein.
FAU - Ishida, N
AU  - Ishida N
AD  - Department of Physiological Chemistry, The Tokyo Metropolitan Institute of
      Medical Science, Bunkyo-ku, Tokyo, 113-8613, Japan.
FAU - Yoshioka, S
AU  - Yoshioka S
FAU - Iida, M
AU  - Iida M
FAU - Sudo, K
AU  - Sudo K
FAU - Miura, N
AU  - Miura N
FAU - Aoki, K
AU  - Aoki K
FAU - Kawakita, M
AU  - Kawakita M
LA  - eng
SI  - GENBANK/AB027147
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - J Biochem
JT  - Journal of biochemistry
JID - 0376600
RN  - 0 (Monosaccharide Transport Proteins)
RN  - 0 (UDP-galactose translocator)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Base Sequence
MH  - CHO Cells
MH  - Cell Line
MH  - Chromosome Banding
MH  - Cloning, Molecular
MH  - Cricetinae
MH  - Golgi Apparatus
MH  - Humans
MH  - In Situ Hybridization, Fluorescence
MH  - Mice
MH  - Molecular Sequence Data
MH  - Monosaccharide Transport Proteins/genetics/*physiology
MH  - Mutagenesis, Site-Directed
MH  - Sequence Deletion
MH  - Structure-Activity Relationship
EDAT- 1999/12/01 09:00
MHDA- 2000/04/01 09:00
CRDT- 1999/12/01 09:00
PHST- 1999/12/01 09:00 [pubmed]
PHST- 2000/04/01 09:00 [medline]
PHST- 1999/12/01 09:00 [entrez]
AID - 10.1093/oxfordjournals.jbchem.a022556 [doi]
PST - ppublish
SO  - J Biochem. 1999 Dec;126(6):1107-17. doi: 10.1093/oxfordjournals.jbchem.a022556.