Canonical Interaction of Cyclin G–associated Kinase with Adaptor Protein 1 Regulates Lysosomal Enzyme Sorting

Kametaka, Satoshi; Moriyama, Kengo; Burgos, Patricia V.; Eisenberg, Evan; Greene, Lois E.; Mattera, Rafael; Bonifacino, Juan S.

doi:10.1091/mbc.e06-12-1162

Cited by 65 publications

(90 citation statements)

References 63 publications

(110 reference statements)

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“…In addition to having a kinase domain, GAK is highly homologous with neuron-specific auxilin, which plays a pivotal role in clathrin-dependent trafficking in neural cells. As expected from this structural similarity, the ubiquitously expressed GAK protein localizes to the trans-Golgi network (TGN) and is an essential cofactor for Hsc70-dependent uncoating of clathrin-coated vesicles in many non-neural cells (Korolchuk and Banting, 2002;Kametaka et al, 2007). Indeed, clathrin-mediated endocytosis is partially blocked in GAK-knockdown cells, and the J domain of GAK was found to be important for this event (Zhang et al, 2005).…”

Section: Introductionmentioning

confidence: 85%

GAK, a regulator of clathrin-mediated membrane traffic, also controls centrosome integrity and chromosome congression

Shimizu

Nagamori

Yabuta

et al. 2009

Journal of Cell Science

102

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Cyclin G-associated kinase (GAK) is an association partner of clathrin heavy chain (CHC) and is essential for clathrinmediated membrane trafficking. Here, we report two novel functions of GAK: maintenance of proper centrosome maturation and of mitotic chromosome congression. Indeed, GAK knockdown by siRNA caused cell-cycle arrest at metaphase, which indicates that GAK is required for proper mitotic progression. We found that this impaired mitotic progression was due to activation of the spindle-assembly checkpoint, which senses protruded, misaligned or abnormally condensed chromosomes in GAK-siRNA-treated cells. GAK knockdown also caused multi-aster formation, which was due to abnormal fragmentation of pericentriolar material, but not of the centrioles. Moreover, GAK and CHC cooperated in the same pathway and interacted in mitosis to regulate the formation of a functional spindle. Taken together, we conclude that GAK and clathrin function cooperatively not only in endocytosis, but also in mitotic progression. Supplementary material available online at

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Section: Introductionmentioning

confidence: 85%

GAK, a regulator of clathrin-mediated membrane traffic, also controls centrosome integrity and chromosome congression

Shimizu

Nagamori

Yabuta

et al. 2009

Journal of Cell Science

102

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“…In addition to its role in endocytosis, GAK has been implicated in delivering lysosomal proteins from TGN (Hirst et al, 2008;Kametaka et al, 2007;Lee et al, 2005;Zhang et al, 2005). In Drosophila, although the importance of clathrinmediated endocytosis in cell-cell signaling and cell morphogenesis RESEARCH ARTICLE Development 138 (6) is well known, the roles of clathrin-dependent transport from organelles in development are less clear.…”

Section: Discussionmentioning

confidence: 99%

“…Alternatively, as we have previously shown that clathrin forms aggregates in aux mutant cells (Kandachar et al, 2008), it is possible that clathrin in these aggregates is incapable of interacting with AP-1. Kametaka et al (Kametaka et al, 2007) have shown that, in HeLa cells, AP-1 recruits GAK to TGN, and the presence of GAK at the TGN is required for lysosomal trafficking. It is possible that, in Drosophila germ cells, localization of Aux to the Golgi also relies on AP-1 and this recruitment is required for formation of CCVs.…”

Section: Discussionmentioning

confidence: 99%

“…In cultured mammalian cells, GAK has been shown to colocalize with Golgi markers in perinuclear regions (Kametaka et al, 2007;Lee et al, 2005). To determine whether Aux localizes to the Golgi in germ cells, b2tub-dAux FL -mRFP testes were stained with antiLva (Lava lamp) and anti-AP-1 antibodies.…”

Section: The Golgi Is Enriched With Auxmentioning

confidence: 99%

“…Within the cell, auxilin family proteins have been suggested to participate in the disassembly of clathrin coats (Gall et al, 2000;Greener et al, 2001;Massol et al, 2006;Pishvaee et al, 2000), recruitment of clathrin and adaptors to membranes (Lee et al, 2005), exchange of clathrin during coatedpit formation Wu et al, 2003), constriction of coated-pits (Newmyer et al, 2003), and prevention of precipitous assembly of clathrin cages (Hirst et al, 2008;Jiang et al, 2000). GAK has also been implicated in mediating trafficking from the trans-Golgi network (TGN) via its interaction with the clathrin adaptor AP-1 (Kametaka et al, 2007).…”

Section: Introductionmentioning

confidence: 99%

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Auxilin is required for formation of Golgi-derived clathrin-coated vesicles during Drosophila spermatogenesis

et al. 2011

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SUMMARYClathrin has previously been implicated in Drosophila male fertility and spermatid individualization. To understand further the role of membrane transport in this process, we analyzed the phenotypes of mutations in Drosophila auxilin (aux), a regulator of clathrin function, in spermatogenesis. Like partial loss-of-function Clathrin heavy chain (Chc) mutants, aux mutant males are sterile and produce no mature sperm. The reproductive defects of aux males were rescued by male germ cell-specific expression of aux, indicating that auxilin function is required autonomously in the germ cells. Furthermore, this rescue depends on both the clathrin-binding and J domains, suggesting that the ability of Aux to bind clathrin and the Hsc70 ATPase is essential for sperm formation. aux mutant spermatids show a deficit in formation of the plasma membrane during elongation, which probably disrupts the subsequent coordinated migration of investment cones during individualization. In wild-type germ cells, GFP-tagged clathrin localized to clusters of vesicular structures near the Golgi. These structures also contained the Golgi-associated clathrin adaptor AP-1, suggesting that they were Golgi-derived. By contrast, in aux mutant cells, clathrin localized to abnormal patches surrounding the Golgi and its colocalization with AP-1 was disrupted. Based on these results, we propose that Golgi-derived clathrin-positive vesicles are normally required for sustaining the plasma membrane increase necessary for spermatid differentiation. Our data suggest that Aux participates in forming these Golgi-derived clathrin-positive vesicles and that Aux, therefore, has a role in the secretory pathway.

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Cell Cycle Control

Matthews¹,

Gerritsen²

2010

Targeting Protein Kinases for Cancer Therapy

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Canonical Interaction of Cyclin G–associated Kinase with Adaptor Protein 1 Regulates Lysosomal Enzyme Sorting

Abstract: The adaptor protein 1 (AP1) complex is a heterotetramer that participates in cargo sorting into clathrin-coated vesicles at the trans-Golgi network (

Cited by 65 publications

References 63 publications

GAK, a regulator of clathrin-mediated membrane traffic, also controls centrosome integrity and chromosome congression

GAK, a regulator of clathrin-mediated membrane traffic, also controls centrosome integrity and chromosome congression

Auxilin is required for formation of Golgi-derived clathrin-coated vesicles during Drosophila spermatogenesis

Cell Cycle Control

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