The autocrine motility factor receptor gene encodes a novel type of seven transmembrane protein<sup>1</sup>

Shimizu, Kimihiro; Tani, Masachika; Watanabe, Hideomi; Nagamachi, Yukio; Niinaka, Yasufumi; Shiroishi, Toshihiko; Ohwada, Susumu; Raz, Avraham; Yokota, Jun

doi:10.1016/s0014-5793(99)00966-7

Cited by 115 publications

(101 citation statements)

References 35 publications

(36 reference statements)

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“…Although previously stated as being a seven-transmembrane (TM) protein [41], detailed analysis of the sequences of mammalian and C. elegans AMFR instead predicts five TM segments (results not shown). This number of TM segments and the presence of a RING finger in AMFR are identical with the architecture of the ER retrotranslocon-associated Saccharomyces cere isiae protein Der3p\Hrd1p, whose RING finger is essential for ER-associated degradation [44].…”

Section: Cue1p a Prototype Of A Novel Domain Familymentioning

confidence: 87%

“…The downstream function of AMFR upon binding AMF is unknown. However the finding of an AMFR CUE domain C-terminal to a previously recognized RINGfinger domain [41] (Figure 2) suggests that AMFR recruits ubiquitination machinery via these two cytoplasmic domains. Really interesting new gene (RING) -finger domains have recently been recognized as binding UBC enzymes and acting as UBCdependent ubiquitin ligases [42].…”

Section: Cue1p a Prototype Of A Novel Domain Familymentioning

confidence: 92%

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Proteins of the endoplasmic-reticulum-associated degradation pathway: domain detection and function prediction

Ponting

2000

Biochemical Journal

113

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Sequence database searches, using iterative-profile and Hidden-Markov-model approaches, were used to detect hitherto-undetected homologues of proteins that regulate the endoplasmic reticulum (ER)-associated degradation pathway. The translocon-associated subunit Sec63p (Sec = secretory) was shown to contain a domain of unknown function found twice in several Brr2p-like RNA helicases (Brr2 = bad response to refrigeration 2). Additionally, Cue1p (Cue=coupling of ubiquitin conjugation to ER degradation), a yeast protein that recruits the ubiquitin-conjugating (UBC) enzyme Ubc7p to an ER-associated complex, was found to be one of a large family of putative scaffolding-domain-containing proteins that include the autocrine motility factor receptor and fungal Vps9p (Vps=vacuolar protein sorting). Two other yeast translocon-associated molecules, Sec72p and Hrd3p (Hrd = 3-hydroxy-3-methylglutaryl-CoA reductase degradation), were shown to contain multiple tetratricopeptide-repeat-like sequences. From this observation it is suggested that Sec72p associates with a heat-shock protein, Hsp70, in a manner analogous to that known for Hop (Hsp70/Hsp90 organizing protein). Finally, the luminal portion of Ire1p (Ire=high inositol-requiring), thought to convey the sensing function of this transmembrane kinase and endoribonuclease, was shown to contain repeats similar to those in β-propeller proteins. This finding hints at the mechanism by which Ire1p may sense extended unfolded proteins at the expense of compact folded molecules.

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Section: Cue1p a Prototype Of A Novel Domain Familymentioning

confidence: 87%

Section: Cue1p a Prototype Of A Novel Domain Familymentioning

confidence: 92%

Proteins of the endoplasmic-reticulum-associated degradation pathway: domain detection and function prediction

Ponting

2000

Biochemical Journal

113

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“…GPI is also known as neuroleukin, a neurotrophic growth factor (53), autocrine motility factor, a stimulator of cell motility and growth (9), and maturation factor, an inducer of differentiation (50). An extracellular receptor for GPI/autocrine motility factor, gp78, has been identified (54). It has been proposed that GPI/autocrine motility factor binds to its receptor through its conserved active site or in a region close to the active site (55).…”

Section: Discussionmentioning

confidence: 99%

Isolation of Novel Animal Cell Lines Defective in Glycerolipid Biosynthesis Reveals Mutations in Glucose-6-phosphate Isomerase

Haller

Smith

Liu

et al. 2010

Journal of Biological Chemistry

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Glycerolipids are structural components for membranes and serve in energy storage. We describe here the use of a photodynamic selection technique to generate a population of Chinese hamster ovary cells that display a global deficiency in glycerolipid biosynthesis. One isolate from this population, GroD1, displayed a profound reduction in the synthesis of phosphatidylcholine, phosphatidylethanolamine, and triglycerides but presented high levels of phosphatidic acid and normal levels of phosphatidylinositol synthesis. This was accompanied by a reduction in phosphatidate phosphatase 1 (PAP1) activity. Expression cloning and sequencing of the cDNA obtained from GroD1 revealed a point mutation, Gly-189 3 Glu, in glucose-6-phosphate isomerase (GPI), a glycolytic enzyme involved in an inherited disorder that results in anemia and neuromuscular symptoms in humans. GPI activity was reduced by 87% in GroD1. No significant differences were found in DNA synthesis, protein synthesis, and ATP levels, whereas glycerol 3-phosphate levels were increased in the mutant. Expression of wild-type hamster GPI restored GPI activity, glycerolipid biosynthesis, and PAP1 activity in GroD1. Two additional, independently isolated GPI-deficient mutants displayed similar phenotypes with respect to PAP1 activity and glycerolipid biosynthesis. These findings uncover a novel relationship between GPI, involved in carbohydrate metabolism, and PAP1, a lipogenic enzyme. These results may also help to explain neuromuscular symptoms associated with inherited GPI deficiency.

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“…15,16 AMF binds to a unique 78 kDa glycoprotein receptor, and initiates gp78 phosphorylation. 4,17 Anti-gp78 monoclonal antibody (3F3A) stimulates motility of metastatic tumor cell, 18 and reveals the localization of gp78 on the leading lamella as well as the trailing edge of motile cells. 19 The expression of gp78 is a predicting factor for prognosis in patients with various malignant neoplasms including esophageal, colorectal, bladder, gastric, and lung carcinoma.…”

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confidence: 99%

Overexpression of autocrine motility factor in metastatic tumor cells: possible association with augmented expression of KIF3A and GDI-β

Yanagawa

Watanabe

Takeuchi

et al. 2004

Laboratory Investigation

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Autocrine motility factor (AMF), which is identical to phosphohexose isomerase (PHI)/glucose-6-phosphate isomerase (GPI) , a ubiquitous enzyme essential for glycolysis, neuroleukin (NLK), a neurotrophic growth factor, and maturation factor (MF) mediating the differentiation of human myeloid cells, enhances the motility and metastatic ability of tumor cells. AMF/PHI activity is elevated in the serum or urine in patients with malignant tumors. Here, we constructed an amf/phi/nlk/mf gene using adenovirus vector and transfected into two tumor cell lines. Overexpression of AMF/PHI/NLK/MF enhanced AMF secretion into the culture media in both tumor cell lines. However, upregulation of motility and metastatic ability was found only in metastatic fibrosarcoma cells expressing an AMF receptor, gp78, and was not found in gp78-undetectable osteosarcoma cells. Thus, not only serum AMF activity but also gp78-expression in tumor cells may be required for metastasis-related motility induction. With the use of microarray analyses, we detected two augmented genes, rho GDP dissociation inhibitor beta and kinesin motor 3A, as well as AMF itself. The RNA message and protein expression of these two molecules was confirmed to be upregulated, suggesting a possible association with AMF-induced signaling for cell motility and metastasis.

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The autocrine motility factor receptor gene encodes a novel type of seven transmembrane protein¹

Cited by 115 publications

References 35 publications

Proteins of the endoplasmic-reticulum-associated degradation pathway: domain detection and function prediction

Proteins of the endoplasmic-reticulum-associated degradation pathway: domain detection and function prediction

Isolation of Novel Animal Cell Lines Defective in Glycerolipid Biosynthesis Reveals Mutations in Glucose-6-phosphate Isomerase

Overexpression of autocrine motility factor in metastatic tumor cells: possible association with augmented expression of KIF3A and GDI-β

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The autocrine motility factor receptor gene encodes a novel type of seven transmembrane protein1

Cited by 115 publications

References 35 publications

Proteins of the endoplasmic-reticulum-associated degradation pathway: domain detection and function prediction

Proteins of the endoplasmic-reticulum-associated degradation pathway: domain detection and function prediction

Isolation of Novel Animal Cell Lines Defective in Glycerolipid Biosynthesis Reveals Mutations in Glucose-6-phosphate Isomerase

Overexpression of autocrine motility factor in metastatic tumor cells: possible association with augmented expression of KIF3A and GDI-β

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The autocrine motility factor receptor gene encodes a novel type of seven transmembrane protein¹