Abstract
Natural resistance to infection with intracellular parasites, such as Leishmania, Salmonella, and Mycobacterium, is controlled in mice by the expression of a single dominant gene locus designated Lsh/Ity/Bcg. Natural resistance-associated macrophage protein gene 1 (NRAMP1) was isolated as a candidate gene. NRAMP1 encodes an M(r) 60000 polypeptide with 10-12 potential transmembrane domains and an evolutionary conserved consensus transport motif. The present study shows that the human NRAMP1 molecule is expressed in all cell lineages of macrophage/monocyte and B- and T-lymphocytes. Immunohistochemical analysis using antihuman NRAMP1 antibody provides the direct evidence that the NRAMP1 molecule is located and distributed on the plasma membrane. An NRAMP1-glutathione S-transferase (GST) fusion protein was used to affinity-purify a protein, bound to the NH2-terminal cytoplasmic domain of NRAMP1. It was found that the NRAMP1 molecule was associated with α- and β-tubulin of microtubules. These results suggest that NRAMP1 may function as a molecule, possessing the abilities of membrane-anchoring and microtubule-binding, for the microtubule-mediated transport of vesicles and be a new class of microtubule-associated proteins.
| Original language | English |
|---|---|
| Pages (from-to) | 1241-1246 |
| Number of pages | 6 |
| Journal | Molecular Immunology |
| Volume | 33 |
| Issue number | 16 |
| DOIs | |
| Publication status | Published - 1996 Nov 1 |
| Externally published | Yes |
Keywords
- natural resistance
- NRAMP1
- subcellular localization
- tubulin
ASJC Scopus subject areas
- Molecular Biology
- Immunology
Cite this
Location of NRAMP1 molecle on the plasma membrane and its association with microtubules. / Kishi, Fumio; Yoshida, Tsutomu; Aiso, Sadakazu.
In: Molecular Immunology, Vol. 33, No. 16, 01.11.1996, p. 1241-1246.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Location of NRAMP1 molecle on the plasma membrane and its association with microtubules
AU - Kishi, Fumio
AU - Yoshida, Tsutomu
AU - Aiso, Sadakazu
PY - 1996/11/1
Y1 - 1996/11/1
N2 - Natural resistance to infection with intracellular parasites, such as Leishmania, Salmonella, and Mycobacterium, is controlled in mice by the expression of a single dominant gene locus designated Lsh/Ity/Bcg. Natural resistance-associated macrophage protein gene 1 (NRAMP1) was isolated as a candidate gene. NRAMP1 encodes an M(r) 60000 polypeptide with 10-12 potential transmembrane domains and an evolutionary conserved consensus transport motif. The present study shows that the human NRAMP1 molecule is expressed in all cell lineages of macrophage/monocyte and B- and T-lymphocytes. Immunohistochemical analysis using antihuman NRAMP1 antibody provides the direct evidence that the NRAMP1 molecule is located and distributed on the plasma membrane. An NRAMP1-glutathione S-transferase (GST) fusion protein was used to affinity-purify a protein, bound to the NH2-terminal cytoplasmic domain of NRAMP1. It was found that the NRAMP1 molecule was associated with α- and β-tubulin of microtubules. These results suggest that NRAMP1 may function as a molecule, possessing the abilities of membrane-anchoring and microtubule-binding, for the microtubule-mediated transport of vesicles and be a new class of microtubule-associated proteins.
AB - Natural resistance to infection with intracellular parasites, such as Leishmania, Salmonella, and Mycobacterium, is controlled in mice by the expression of a single dominant gene locus designated Lsh/Ity/Bcg. Natural resistance-associated macrophage protein gene 1 (NRAMP1) was isolated as a candidate gene. NRAMP1 encodes an M(r) 60000 polypeptide with 10-12 potential transmembrane domains and an evolutionary conserved consensus transport motif. The present study shows that the human NRAMP1 molecule is expressed in all cell lineages of macrophage/monocyte and B- and T-lymphocytes. Immunohistochemical analysis using antihuman NRAMP1 antibody provides the direct evidence that the NRAMP1 molecule is located and distributed on the plasma membrane. An NRAMP1-glutathione S-transferase (GST) fusion protein was used to affinity-purify a protein, bound to the NH2-terminal cytoplasmic domain of NRAMP1. It was found that the NRAMP1 molecule was associated with α- and β-tubulin of microtubules. These results suggest that NRAMP1 may function as a molecule, possessing the abilities of membrane-anchoring and microtubule-binding, for the microtubule-mediated transport of vesicles and be a new class of microtubule-associated proteins.
KW - natural resistance
KW - NRAMP1
KW - subcellular localization
KW - tubulin
UR - http://www.scopus.com/inward/record.url?scp=0030273839&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0030273839&partnerID=8YFLogxK
U2 - 10.1016/S0161-5890(96)00088-0
DO - 10.1016/S0161-5890(96)00088-0
M3 - Article
C2 - 9129160
AN - SCOPUS:0030273839
VL - 33
SP - 1241
EP - 1246
JO - Molecular Immunology
JF - Molecular Immunology
SN - 0161-5890
IS - 16
ER -