Regulation of endocytic traffic by Rho GTPases

Qualmann, Britta; Mellor, Harry

doi:10.1042/bj20030139

Cited by 116 publications

(104 citation statements)

References 115 publications

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“…Although the Rab and Arf families of GTPases are best known for their roles in vesicle budding, docking, fusion, and movement within the mammalian endocytic and secretory pathways (45)(46)(47), functions for the Rho family of GTPases in vesicle pathways are being elucidated (48). A role for Cdc42 in intracellular trafficking in yeast has been identified, where Cdc42 is involved in vacuolar membrane docking and fusion (49,50).…”

Section: Discussionmentioning

confidence: 99%

FGD2, a CDC42-specific Exchange Factor Expressed by Antigen-presenting Cells, Localizes to Early Endosomes and Active Membrane Ruffles

Huber¹,

Mårtensson²,

Bokoch

et al. 2008

Journal of Biological Chemistry

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Members of the Fgd (faciogenital dysplasia) gene family encode a group of critical guanine nucleotide exchange factors (GEFs), which, by specifically activating Cdc42, control cytoskeleton-dependent membrane rearrangements. In its first characterization, we find that FGD2 is expressed in antigen-presenting cells, including B lymphocytes, macrophages, and dendritic cells. In the B lymphocyte lineage, FGD2 levels change with developmental stage. In both mature splenic B cells and immature bone marrow B cells, FGD2 expression is suppressed upon activation through the B cell antigen receptor. FGD2 has a complex intracellular localization, with concentrations found in membrane ruffles and early endosomes. Although endosomal localization of FGD2 is dependent on a conserved FYVE domain, its C-terminal pleckstrin homology domain mediates recruitment to membrane ruffles. FGD2 overexpression promotes the activation of Cdc42 and leads to elevated JNK1 activity in a Cdc42-but not Rac1-dependent fashion. These findings are consistent with a role of FGD2 in leukocyte signaling and vesicle trafficking in cells specialized to present antigen in the immune system.

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Section: Discussionmentioning

confidence: 99%

FGD2, a CDC42-specific Exchange Factor Expressed by Antigen-presenting Cells, Localizes to Early Endosomes and Active Membrane Ruffles

Huber¹,

Mårtensson²,

Bokoch

et al. 2008

Journal of Biological Chemistry

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“…Furthermore, we demonstrated that these effects in the non-malignant and malignant cell lines were reversed when the cells were grown on fibronectin such that EGF-induced receptor internalization was reduced with MCF-10A cells but enhanced in the T47D cells. Rho is known to play a key role in endocytic trafficking (35), and it has been shown previously that internalization of EGFR can be Rho-dependent (36,37). With MCF-10A cells, we found that IGFBP-3 activated Rho after 2 min, which was maximal at 5 min.…”

Section: Igfbp-3 Has Differential Effects On Egf-induced Cellmentioning

confidence: 48%

IGFBP-3 Can Either Inhibit or Enhance EGF-mediated Growth of Breast Epithelial Cells Dependent upon the Presence of Fibronectin

McIntosh¹,

Dennison²,

Holly

et al. 2010

Journal of Biological Chemistry

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Progression of breast cancer is associated with remodeling of the extracellular matrix, often involving a switch from estrogen dependence to a dependence on EGF receptor (EGFR)/HER-2 and is accompanied by increased expression of the main binding protein for insulin-like growth factors (IGFBP-3). We have examined the effects of IGFBP-3 on EGF responses of breast epithelial cells in the context of changes in the extracellular matrix. On plastic and laminin with MCF-10A normal breast epithelial cells, EGF and IGFBP-3 each increased cell growth and together produced a synergistic response, whereas with T47D breast cancer cells IGFBP-3 alone had no effect, but the ability of EGF to increase cell proliferation was markedly inhibited in the presence of IGFBP-3. In contrast on fibronectin with MCF-10A cells, IGFBP-3 alone inhibited cell growth and blocked EGF-induced proliferation. With the cancer cells, IGFBP-3 alone had no effect but enhanced the EGF-induced increase in cell growth. The insulin-like growth factor-independent effects of IGFBP-3 alone on cell proliferation were completely abrogated in the presence of an EGFR, tyrosine kinase inhibitor, Iressa. Although IGFBP-3 did not affect EGFR phosphorylation [Tyr 1068 ], it was found to modulate receptor internalization and was associated with activation of Rho and subsequent changes in MAPK phosphorylation. The levels of fibronectin and IGFBP-3 within breast tumors may determine their dependence on EGFR and their response to therapies targeting this receptor.

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“…Elles jouent un rôle essentiel dans des processus cellulaires variés incluant la migration cellulaire, l'adhérence, la phagocytose, grâce à la régulation de l'activité de nombreuses protéines effectrices contrôlant l'assemblage et l'organisation des filaments d'actine [7]. Récemment, plusieurs membres de cette famille ont également été impliqués dans la régula-tion du trafic intracellulaire [8]. [9][10][11].…”

Section: Un Relais Entre Les Protéines G Arf1 Et Cdc42unclassified

Une nouvelle protéine RhoGAP impliquée dans la régulation du complexe Arp2/3 au niveau de l’appareil de Golgi : Un relais entre les protéines G ARF1 et Cdc42

Dubois

Chavrier

2005

Med Sci (Paris)

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Regulation of endocytic traffic by Rho GTPases

Cited by 116 publications

References 115 publications

FGD2, a CDC42-specific Exchange Factor Expressed by Antigen-presenting Cells, Localizes to Early Endosomes and Active Membrane Ruffles

FGD2, a CDC42-specific Exchange Factor Expressed by Antigen-presenting Cells, Localizes to Early Endosomes and Active Membrane Ruffles

IGFBP-3 Can Either Inhibit or Enhance EGF-mediated Growth of Breast Epithelial Cells Dependent upon the Presence of Fibronectin

Une nouvelle protéine RhoGAP impliquée dans la régulation du complexe Arp2/3 au niveau de l’appareil de Golgi : Un relais entre les protéines G ARF1 et Cdc42

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