1995
DOI: 10.1074/jbc.270.40.23612
|View full text |Cite
|
Sign up to set email alerts
|

Cloning and Characterization of a Novel Insulin-regulated Membrane Aminopeptidase from Glut4 Vesicles

Abstract: The insulin-regulated glucose transporter isotype GluT4 expressed only in muscle and adipose cells is sequestered in a specific secretory vesicle. These vesicles harbor another major protein, referred to as vp165 (for vesicle protein of 165 kDa), that like GluT4 redistributes to the plasma membrane in response to insulin. We describe here the cloning of vp165 and show that it is a novel member of the family of zinc-dependent membrane aminopeptidases, with the typical large extracellular catalytic domain and si… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
1

Citation Types

4
308
0
3

Year Published

1997
1997
2016
2016

Publication Types

Select...
6
2

Relationship

0
8

Authors

Journals

citations
Cited by 300 publications
(315 citation statements)
references
References 36 publications
4
308
0
3
Order By: Relevance
“…The first two are the IGF-II/Man-6-phosphate receptor (8) and IRAP, respectively (6,7,17). To identify gp110, we isolated adipocytes from 60 rats, prepared the light microsomal fraction from these cells (see "Materials and Methods") and immunoadsorbed Glut4-containing vesicles.…”
Section: Resultsmentioning
confidence: 99%
“…The first two are the IGF-II/Man-6-phosphate receptor (8) and IRAP, respectively (6,7,17). To identify gp110, we isolated adipocytes from 60 rats, prepared the light microsomal fraction from these cells (see "Materials and Methods") and immunoadsorbed Glut4-containing vesicles.…”
Section: Resultsmentioning
confidence: 99%
“…We are currently unable to distinguish these two possibilities, and further experimentation is required to address this question in the future. It is well known that the other protein residing in GSVs, IRAP, traffics together with GLUT4 in response to insulin (40), and its expression is decreased in various GLUT4-null cells (41,42). Interestingly, in contrast to GLUT4, IRAP levels were normal in tissues or primary adipocytes from the AS160 KO mice, suggesting that the degradation of these two proteins might be differentially regulated.…”
mentioning
confidence: 99%
“…Insulin-responsive aminopeptidase (IRAP) was identified as an abundant cargo protein associated with GLUT4 vesicles that translocates in response to insulin in a manner seemingly identical to GLUT4 Mastick et al, 1994;Keller et al, 1995;Malide et al, 1997;Martin et al, 1997;Ross et al, 1997). In fact, it is more abundantly expressed in vesicles than the transporter (Kupriyanova et al, 2002).…”
Section: Introductionmentioning
confidence: 99%
“…All this strongly suggests the involvement of IRAP with the retention and sorting machinery of GSVs and its potential association with the targeting and tethering proteins involved in this process. IRAP has a single transmembrane domain with the Nterminus projecting into the cytosol (Keller et al, 1995), whereas GLUT4 has potential sorting and targeting motifs in three cytosolic domains corresponding to N-and C-termini as well as the central loop that connects helices 6 and 7 (Fukumoto et al, 1989). The N-terminus of IRAP has dileucine motifs and an acidic cluster domain similar to that found in the C-terminus of GLUT4, which is thought to be important region for its trafficking (Verhey et al, 1993(Verhey et al, , 1995Corvera et al, 1994;Verhey and Birnbaum, 1994;Haney et al, 1995;Marsh et al, 1995).…”
Section: Introductionmentioning
confidence: 99%
See 1 more Smart Citation