SNX4 coordinates endosomal sorting of TfnR with dynein-mediated transport into the endocytic recycling compartment

Traer, Colin J.; Rutherford, Anna C.; Palmer, Krysten J.; Wassmer, Thomas; Oakley, Jacqueline; Attar, Naomi; Carlton, Jeremy G.; Kremerskothen, Joachim; Stephens, David; Cullen, Peter J.

doi:10.1038/ncb1656

Cited by 243 publications

(316 citation statements)

References 41 publications

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“…30 -32 In addition to the putative indirect association to the actin cytoskeleton, it has been demonstrated that KIBRA directly binds to dynein light chain 1 (DLC1) and sorting nexin 4 (SNX4). 38,39 The DLC1-SNX4-KIBRA complex associates with the minus-end directed microtubule motor dynein complex. 38 These studies support our observation that KIBRA at least indirectly associates with the microtubule network; therefore, KIBRA might act as a bridge between actin-and/or microtubule-associated networks and cell polarity complexes.…”

Section: Discussionmentioning

confidence: 99%

KIBRA Modulates Directional Migration of Podocytes

Duning¹,

Schurek²,

Schlüter³

et al. 2008

Journal of the American Society of Nephrology

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Asymmetric delivery and distribution of macromolecules are essential for cell polarity and for cellular functions such as differentiation, division, and signaling. Injury of podocytes, which are polarized epithelial cells, changes the dynamics of the actin meshwork, resulting in foot process retraction and proteinuria. Although the spatiotemporal control of specific protein-protein interactions is crucial for the establishment of cell polarity, the mechanisms controlling polarity-dependent differentiation and division are incompletely understood. In this study, yeast two-hybrid screens were performed using a podocyte cDNA library and the polarity protein PATJ as bait. The protein KIBRA was identified as an interaction partner of PATJ and was localized to podocytes, tubular structures, and collecting ducts. The last four amino acids of KIBRA mediated binding to the eighth PDZ domain of PATJ. In addition, KIBRA directly bound to synaptopodin, an essential organizer of the podocyte cytoskeleton. Stable knockdown of KIBRA in immortalized podocytes impaired directed cell migration, suggesting that KIBRA modulates the motility of podocytes by linking polarity proteins and cytoskeleton-associated protein complexes.

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Section: Discussionmentioning

confidence: 99%

KIBRA Modulates Directional Migration of Podocytes

Duning¹,

Schurek²,

Schlüter³

et al. 2008

Journal of the American Society of Nephrology

Self Cite

111

140

View full text Add to dashboard Cite

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“…Accumulating evidence suggests that cytoskeletons have profound roles guiding and segregating membrane trafficking intermediates (5,(47)(48)(49). To further unravel the machinery underlying the dynamic hTAC tubules, we tested their dependence on the cytoskeleton.…”

Section: The Generation Of Htac-positive Tubules Requires Microtubulementioning

confidence: 99%

SEC-10 and RAB-10 coordinate basolateral recycling of clathrin-independent cargo through endosomal tubules in Caenorhabditis elegans

Chen

et al. 2014

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

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Despite the increasing number of regulatory proteins identified in clathrin-independent endocytic (CIE) pathways, our understanding of the exact functions of these proteins and the sequential manner in which they function remains limited. In this study, using the Caenorhabditis elegans intestine as a model, we observed a unique structure of interconnected endosomal tubules, which is required for the basolateral recycling of several CIE cargoes including hTAC, GLUT1, and DAF-4. SEC-10 is a subunit of the octameric protein complex exocyst. Depleting SEC-10 and several other exocyst components disrupted the endosomal tubules into various ring-like structures. An epistasis analysis further suggested that SEC-10 operates at the intermediate step between early endosomes and recycling endosomes. The endosomal tubules were also sensitive to inactivation of the Rab GTPase RAB-10 and disruption of microtubules. Taken together, our data suggest that SEC-10 coordinates with RAB-10 and microtubules to form the endosomal tubular network for efficient recycling of particular CIE cargoes.endosomal tubules | recycling | microtubule | clathrin-independent endocytosis | live worm imaging

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“…SNX3 binds to PI(3)P [16] and is required for biogenesis of endocytic carrier vesicles/multivesicular bodies [17]. SNX4 associates with dynein/dynactin through its interaction with the dynein light chain 1-binding protein KIBRA and is required for transport of the transferrin receptor between peripheral early endosomes and the juxtanuclear endocytic recycling compartment [18]. SNX9, in contrast, senses phosphatidylinositol 4,5-bisphosphate signals at the plasma membrane and couples actin dynamics with membrane remodeling during clathrin-mediated endocytosis, dorsal ruffle formation and clathrin-independent fluid phase endocytosis [19].…”

Section: Introductionmentioning

confidence: 99%

The retromer component SNX6 interacts with dynactin p150Glued and mediates endosome-to-TGN transport

et al. 2009

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The retromer is a protein complex that mediates retrograde transport of transmembrane cargoes from endosomes to the trans-Golgi network (TGN). It is comprised of a cargo-selection subcomplex of Vps26, Vps29 and Vps35 and a membrane-binding coat subcomplex of sorting nexins (SNXs). Previous studies identified SNX1/2 as one of the components of the SNX subcomplex, and SNX5/6 as candidates for the second SNX. How the retromer-associated cargoes are recognized and transported by molecular motors are largely unknown. In this study, we found that one of SNX1/2's dimerization partners, SNX6, interacts with the p150 Glued subunit of the dynein/dynactin motor complex. We present evidence that SNX6 is a component of the retromer, and that recruitment of the motor complex to the membrane-associated retromer requires the SNX6-p150 Glued interaction. Disruption of the SNX6-p150 Glued interaction causes failure in formation and detachment of the tubulovesicular sorting structures from endosomes and results in block of CI-MPR retrieval from endosomes to the TGN. These observations indicate that in addition to SNX1/2, SNX6 in association with the dynein/dynactin complex drives the formation and movement of tubular retrograde intermediates.

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SNX4 coordinates endosomal sorting of TfnR with dynein-mediated transport into the endocytic recycling compartment

Cited by 243 publications

References 41 publications

KIBRA Modulates Directional Migration of Podocytes

KIBRA Modulates Directional Migration of Podocytes

SEC-10 and RAB-10 coordinate basolateral recycling of clathrin-independent cargo through endosomal tubules in Caenorhabditis elegans

The retromer component SNX6 interacts with dynactin p150Glued and mediates endosome-to-TGN transport

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