Millipore Sigma Vibrant Logo
 

Rab


330 Results Erweiterte Suche  
Suchergebnisse
Produkte (49)
Dokumente (277)
Seiten (4)

Suche eingrenzen Grenzen Sie Ihre Suche mit den nachstehenden Filtern ein

Dokumententyp

  • (158)
  • (116)
  • (3)
Finden Sie nicht, was Sie suchen?
Kontaktieren Sie bitten
den Kundenservice

 
Benötigen Sie Hilfe, um ein Dokument zu finden?
  • Verwenden Sie die Dokumentensuche, um nach Analysenzertifikaten, Qualitätszertifikaten oder Sicherheitsdatenblättern zu suchen.
  • Wenn Sie bei der Suche einer Gebrauchsanleitung oder eines Benutzerhandbuchs Hilfe benötigen, kontaktieren Sie bitte den Kundenservice.

  • Rab proteins mediate Golgi transport of caveola-internalized glycosphingolipids and correct lipid trafficking in Niemann-Pick C cells. 12070301

    We recently showed that human skin fibroblasts internalize fluorescent analogues of the glycosphingolipids lactosylceramide and globoside almost exclusively by a clathrin-independent mechanism involving caveolae. In contrast, a sphingomyelin analogue is internalized approximately equally via clathrin-dependent and caveolar routes. Here, we further characterized the caveolar pathway for glycosphingolipids, showing that Golgi targeting of sphingolipids internalized via caveolae required microtubules and phosphoinositol 3-kinases and was inhibited in cells expressing dominant-negative Rab7 and Rab9 constructs. In addition, overexpression of wild-type Rab7 or Rab9 (but not Rab11) in Niemann-Pick type C (NP-C) lipid storage disease fibroblasts resulted in correction of lipid trafficking defects, including restoration of Golgi targeting of fluorescent lactosylceramide and endogenous GM(1) ganglioside, and a dramatic reduction in intracellular cholesterol stores. Our results demonstrate a role for Rab7 and Rab9 in the Golgi targeting of glycosphingolipids and suggest a new therapeutic approach for restoring normal lipid trafficking in NP-C cells.
    Dokumententyp:
    Referenz
    Produkbestellnummer:
    05-853

  • Rab GTPase-activating proteins in autophagy: regulation of endocytic and autophagy pathways by direct binding to human ATG8 modifiers. 22354992

    Autophagy is an evolutionarily conserved degradation pathway characterized by dynamic rearrangement of membranes that sequester cytoplasm, protein aggregates, organelles, and pathogens for delivery to the vacuole and lysosome, respectively. The ability of autophagosomal membranes to act selectively toward specific cargo is dependent on the small ubiquitin-like modifier ATG8/LC3 and the LC3-interacting region (LIR) present in autophagy receptors. Here, we describe a comprehensive protein-protein interaction analysis of TBC (Tre2, Bub2, and Cdc16) domain-containing Rab GTPase-activating proteins (GAPs) as potential autophagy adaptors. We identified 14 TBC domain-containing Rab GAPs that bind directly to ATG8 modifiers and that colocalize with LC3-positive autophagy membranes in cells. Intriguingly, one of our screening hits, TBC1D5, contains two LIR motifs. The N-terminal LIR was critical for interaction with the retromer complex and transport of cargo. Direct binding of the retromer component VPS29 to TBC1D5 could be titrated out by LC3, indicating a molecular switch between endosomes and autophagy. Moreover, TBC1D5 could bridge the endosome and autophagosome via its C-terminal LIR motif. During starvation-induced autophagy, TBC1D5 was relocalized from endosomal localization to the LC3-positive autophagosomes. We propose that LC3-interacting Rab GAPs are implicated in the reprogramming of the endocytic trafficking events under starvation-induced autophagy.
    Dokumententyp:
    Referenz
    Produkbestellnummer:
    ABC432
    Produktbezeichnung:
    Anti-LC3B Antibody

  • Calmodulin binds to the Rab GTPase activating protein required for insulin-stimulated GLUT4 translocation. 16055084

    Recently, we described a 160 kDa protein with a Rab GTPase activating protein domain that is phosphorylated on multiple sites by the protein kinase Akt (designated AS160). Phosphorylation of AS160 in adipocytes is required for insulin-stimulated translocation of the glucose transporter GLUT4 to the plasma membrane. In the present study, we searched for proteins that interact with the GTPase activating protein (GAP) domain region of AS160 by the yeast two-hybrid screen. This search indicated that calmodulin bound to a small domain just amino terminal to the GAP domain of AS160, and this association has been confirmed by three other methods, including co-immunoprecipitation from lysates of adipocytes. The association was Ca ion dependent. The role of calmodulin binding to AS160 in insulin-stimulated GLUT4 translocation was examined through the generation of a point mutant of AS160 that did not bind calmodulin. This mutation did not interfere with the capacity of AS160 lacking Akt phosphorylation sites to inhibit GLUT4 translocation. Consequently, calmodulin binding is probably not required for the participation of AS160 in insulin-stimulated GLUT4 translocation.
    Dokumententyp:
    Referenz
    Produkbestellnummer:
    05-173
    Produktbezeichnung:
    Anti-Calmodulin Antibody

  • Inhibition of GLUT4 translocation by Tbc1d1, a Rab GTPase-activating protein abundant in skeletal muscle, is partially relieved by AMP-activated protein kinase activation ... 18258599

    Insulin increases glucose transport by stimulating the trafficking of intracellular GLUT4 to the cell surface, a process known as GLUT4 translocation. A key protein in signaling this process is AS160, a Rab GTPase-activating protein (GAP) whose activity appears to be suppressed by Akt phosphorylation. Tbc1d1 is a Rab GAP with a sequence highly similar to that of AS160 and with the same Rab specificity as that of AS160. The role of Tbc1d1 in regulating GLUT4 trafficking has been unclear. Our previous study showed that overexpressed Tbc1d1 inhibited insulin-stimulated GLUT4 translocation in 3T3-L1 adipocytes, even though insulin caused phosphorylation on its single canonical Akt motif. In the present study, we show in 3T3-L1 adipocytes that Tbc1d1 is only 1/20 as abundant as AS160, that knockdown of Tbc1d1 has no effect on insulin-stimulated GLUT4 translocation, and that overexpressed Tbc1d1 also inhibits GLUT4 translocation elicited by activated Akt expression. These results indicate that endogenous Tbc1d1 does not participate in insulin-regulated GLUT4 translocation in adipocytes and suggest that the GAP activity of Tbc1d1 is not suppressed by Akt phosphorylation. In addition, we discovered that Tbc1d1 is much more highly expressed in skeletal muscle than fat and that the AMP-activated protein kinase (AMPK) activator 5'-aminoimidazole-4-carboxamide ribonucleoside partially reversed the inhibition of insulin-stimulated GLUT4 translocation by overexpressed Tbc1d1 in 3T3-L1 adipocytes. 5'-Aminoimidazole-4-carboxamide ribonucleoside activation of the kinase AMPK is known to cause GLUT4 translocation in muscle. The above findings strongly suggest that Tbc1d1 is a component in the signal transduction pathway leading to AMPK-stimulated GLUT4 translocation in muscle.
    Dokumententyp:
    Referenz
    Produkbestellnummer:
    06-549
    Produktbezeichnung:
    Anti-Myc Tag Antibody

  • Anti-AS160 (Rab GAP) - 30554

    Dokumententyp:
    Analysenzertifikat
    Chargennummer:
    30554
    Produkbestellnummer:
    07-741
    Produktbezeichnung:
    Anti-AS160 (Rab-GAP) Antibody