Insulin responsiveness of glucose transporter 4 in 3T3-L1 cells depends on the presence of sortilin

Autor: Jun-Jun Shi, Tessa D. Nauta, Konstantin V. Kandror, Agnes Asmar, Ju-Youn Kim, Guanrong Huang, Dana Buckler-Pena, Maneet Singh
Rok vydání: 2013
Předmět:
Blood Glucose
medicine.medical_specialty
endocrine system diseases
medicine.medical_treatment
Cellular differentiation
Proto-Oncogene Proteins c-myc
Mice
03 medical and health sciences
0302 clinical medicine
3T3-L1 Cells
Internal medicine
Diabetes mellitus
Adipocytes
medicine
Animals
Humans
Insulin
Molecular Biology
030304 developmental biology
0303 health sciences
Glucose Transporter Type 4
biology
Cell Membrane
Glucose transporter
nutritional and metabolic diseases
Skeletal muscle
Cell Differentiation
Articles
Cell Biology
musculoskeletal system
medicine.disease
Adaptor Proteins
Vesicular Transport
Endocrinology
medicine.anatomical_structure
Postprandial
Gene Expression Regulation
Membrane Trafficking
biology.protein
hormones
hormone substitutes
and hormone antagonists
030217 neurology & neurosurgery
GLUT4
Zdroj: Molecular Biology of the Cell
ISSN: 1939-4586
1059-1524
DOI: 10.1091/mbc.e12-10-0765
Popis: Insulin-dependent translocation of Glut4 to the plasma membrane of fat and skeletal muscle cells plays the key role in postprandial clearance of blood glucose. In undifferentiated cells, insulin responsiveness of Glut4 depends on the presence of sortilin, whereas sortilin responds to insulin regardless of Glut4 expression.
Insulin-dependent translocation of glucose transporter 4 (Glut4) to the plasma membrane of fat and skeletal muscle cells plays the key role in postprandial clearance of blood glucose. Glut4 represents the major cell-specific component of the insulin-responsive vesicles (IRVs). It is not clear, however, whether the presence of Glut4 in the IRVs is essential for their ability to respond to insulin stimulation. We prepared two lines of 3T3-L1 cells with low and high expression of myc7-Glut4 and studied its translocation to the plasma membrane upon insulin stimulation, using fluorescence-assisted cell sorting and cell surface biotinylation. In undifferentiated 3T3-L1 preadipocytes, translocation of myc7-Glut4 was low regardless of its expression levels. Coexpression of sortilin increased targeting of myc7-Glut4 to the IRVs, and its insulin responsiveness rose to the maximal levels observed in fully differentiated adipocytes. Sortilin ectopically expressed in undifferentiated cells was translocated to the plasma membrane regardless of the presence or absence of myc7-Glut4. AS160/TBC1D4 is expressed at low levels in preadipocytes but is induced in differentiation and provides an additional mechanism for the intracellular retention and insulin-stimulated release of Glut4.
Databáze: OpenAIRE
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