ACAP1 Promotes Endocytic Recycling by Recognizing Recycling Sorting Signals

Dai, Jun; Li, Jian; Bos, Erik; Porcionatto, Marimélia; Premont, Richard T.; Bourgoin, Sylvain G.; Peters, Peter J.; Hsu, Victor

doi:10.1016/j.devcel.2004.10.002

Cited by 105 publications

(137 citation statements)

References 21 publications

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“…How imatinib facilitates TfR1-Hsc70 interaction and trafficking to the lysosome for degradation is unclear. Perhaps most relevant is the well documented identification of two distinct phenylalanine-based sequences in the cytoplasmic TfR1 tail that recruits the ARF6 GTPase-activating protein called ACAP1 (39). Importantly, this interaction appears to promote cargo sorting of GLUT4 as well as both TfR1 and the integrin receptors (6).…”

Section: Discussionmentioning

confidence: 99%

The Endocytic Fate of the Transferrin Receptor Is Regulated by c-Abl Kinase

Cao

Schroeder

Chen

et al. 2016

Journal of Biological Chemistry

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Clathrin-mediated endocytosis of transferrin (Tf) and its cognate receptor (TfR1) is a central pathway supporting the uptake of trophic iron. It has generally been assumed that this is a constitutive process. However, we have reported that the non-receptor tyrosine kinase, Src, is activated by Tf to facilitate the internalization of the Tf-TfR1 ligand-receptor complex. As an extension of these findings, we have tested whether subsequent trafficking steps might be regulated by additional kinase-dependent cascades, and we observed a significant endocytic block by inhibiting c-Abl kinase by a variety of methods. Importantly, Tf internalization was reduced significantly in all of these cell models and could be restored by re-expression of WT c-Abl. Surprisingly, this attenuated Tf-TfR1 endocytosis was due to a substantial drop in both the surface and total cellular receptor levels. Additional studies with the LDL receptor showed a similar effect. Surprisingly, immunofluorescence microscopy of imatinib-treated cells revealed a marked colocalization of internalized TfR1 with late endosomes/lysosomes, whereas attenuating the lysosome function with several inhibitors reduced this receptor loss. Importantly, inhibition of c-Abl resulted in a striking redistribution of the chaperone Hsc70 from a diffuse cytosolic localization to an association with the TfR1 at the late endosome-lysosome. Pharmacological inhibition of Hsc70 ATPase activity in cultured cells by the drug VER155008 prevents this chaperone-receptor interaction, resulting in an accumulation of the TfR1 in the early endosome. Thus, inhibition of c-Abl minimizes receptor recycling pathways and results in chaperone-dependent trafficking of the TfR1 to the lysosome for degradation. These findings implicate a novel role for c-Abl and Hsc70 as an unexpected regulator of Hsc70-mediated transport of trophic receptor cargo between the early and late endosomal compartments.

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Section: Discussionmentioning

confidence: 99%

The Endocytic Fate of the Transferrin Receptor Is Regulated by c-Abl Kinase

Cao

Schroeder

Chen

et al. 2016

Journal of Biological Chemistry

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“…Rab/Arf cross-talk is likely important for many higherlevel processes that depend upon tight regulation of recycling endosome function. Previous studies in mammals demonstrated a role for ACAP1 in Glut4 and integrin recycling (39,40). Furthermore, ACAP1 was reported to be part of a clathrin-coat complex on endosomes (31).…”

Section: Discussionmentioning

confidence: 99%

RAB-10-GTPase–mediated regulation of endosomal phosphatidylinositol-4,5-bisphosphate

Shi

Liu²,

Koenig

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

108

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Caenorhabditis elegans RAB-10 and mammalian Rab10 are key regulators of endocytic recycling, especially in the basolateral recycling pathways of polarized epithelial cells. To understand better how RAB-10 contributes to recycling endosome function, we sought to identify RAB-10 effectors. One RAB-10-binding partner that we identified, CNT-1, is the only C. elegans homolog of the mammalian Arf6 GTPase-activating proteins ACAP1 and ACAP2. Arf6 is known to regulate endosome-to-plasma membrane transport, in part through activation of type I phophatidylinositol-4-phosphate 5 kinase. Here we show that CNT-1 binds to RAB-10 through its C-terminal ankyrin repeats and colocalizes with RAB-10 and ARF-6 on recycling endosomes in vivo. Furthermore, we find that RAB-10 is required for the recruitment of CNT-1 to endosomal membranes in the intestinal epithelium. Consistent with negative regulation of ARF-6 by RAB-10 and CNT-1, we found overaccumulation of endosomal phosphatidylinositol-4,5-bisphosphate [PI(4,5)P2] in cnt-1 and rab-10 mutants and reduced endosomal PI(4,5)P2 levels in arf-6 mutants. These mutants produced similar effects on endosomal recruitment of the PI(4,5)P2-dependent membrane-bending proteins RME-1/Ehd and SDPN-1/Syndapin/Pacsin and resulted in endosomal trapping of specific recycling cargo. Our studies identify a RAB-10-to-ARF-6 regulatory loop required to regulate endosomal PI(4,5)P2, a key phosphoinositide in membrane traffic. membrane lipid | clathrin

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“…Mouse anti-GFP and rabbit anti-GAPDH antibodies were obtained from Covance. Alexa Fluor 488-conjugated Tf has been described (27).…”

Section: Methodsmentioning

confidence: 99%

“…Equilibrium centrifugation using sucrose gradients was performed essentially as described (14), except total cell homogenate rather than Golgi-enriched fraction was loaded at the bottom of the gradient for floatation analysis. TfR internalization assay was performed as described (27).…”

Section: Methodsmentioning

confidence: 99%

A role for the host coatomer and KDEL receptor in early vaccinia biogenesis

Zhang

Lee

Beznoussenko

et al. 2009

Proc. Natl. Acad. Sci. U.S.A.

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Members of the poxvirus family have been investigated for their applications as vaccines and expression vectors and, more recently, because of concern for their potential as biological weapons. Vaccinia virus, the prototypic member, evolves through multiple forms during its replication. Here, we show a surprising way by which vaccinia hijacks coatomer for early viral biogenesis. Whereas coatomer forms COPI vesicles in the host early secretory system, vaccinia formation bypasses this role of coatomer, but instead, depends on coatomer interacting with the host KDEL receptor. To gain insight into the viral roles of these two host proteins, we have detected them on the earliest recognized viral forms. These findings not only suggest insights into early vaccinia biogenesis but also reveal an alternate mechanism by which coatomer acts.COPI ͉ morphogenesis

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ACAP1 Promotes Endocytic Recycling by Recognizing Recycling Sorting Signals

Cited by 105 publications

References 21 publications

The Endocytic Fate of the Transferrin Receptor Is Regulated by c-Abl Kinase

The Endocytic Fate of the Transferrin Receptor Is Regulated by c-Abl Kinase

RAB-10-GTPase–mediated regulation of endosomal phosphatidylinositol-4,5-bisphosphate

A role for the host coatomer and KDEL receptor in early vaccinia biogenesis

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