Regulation of protein trafficking: JNK3 at the Golgi complex

Yang, Guang; Cynader, Max S.

doi:10.4161/cc.27019

Cited by 7 publications

(6 citation statements)

References 7 publications

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“…c‐Jun N‐terminal kinase 3 (JNK3) is a MAPK and JNK p54 isoform that is abundant in the brain and important for the neuronal stress response . Excitotoxicity in primary rat neurons causes JNK3 to accumulate at the Golgi, where it binds and recruits Sac1, leading to decreased Golgi PI4P and reduced secretory trafficking . Other mammalian JNK isoforms contain homologous sequences that could perform an analogous function in cell types where JNK3 is absent .…”

Section: Sac1 Function In Different Intracellular Compartmentsmentioning

confidence: 99%

“…95,96 Excitotoxicity in primary rat neurons causes JNK3 to accumulate at the Golgi, where it binds and recruits Sac1, leading to decreased Golgi PI4P and reduced secretory trafficking. [97][98][99] Other mammalian JNK isoforms contain homologous sequences that could perform an analogous function in cell types where JNK3 is absent. 98 Thus, whereas p38 MAPK targets mammalian Sac1 to the ER and drives anterograde trafficking in response to growth factors, JNK3 MAPK traps Sac1 at the Golgi, thereby preventing anterograde trafficking in response to neuronal stress.…”

Section: Er-to-golgi Shuttling Of Sac1 In Mammalian Cells Is Controllmentioning

confidence: 99%

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Sac1, a lipid phosphatase at the interface of vesicular and nonvesicular transport

Bel

Brill

2018

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The lipid phosphatase Sac1 dephosphorylates phosphatidylinositol 4-phosphate (PI4P), thereby holding levels of this crucial membrane signaling molecule in check. Sac1 regulates multiple cellular processes, including cytoskeletal organization, membrane trafficking and cell signaling. Here, we review the structure and regulation of Sac1, its roles in cell signaling and development and its links to health and disease. Remarkably, many of the diverse roles attributed to Sac1 can be explained by the recent discovery of its requirement at membrane contact sites, where its consumption of PI4P is proposed to drive interorganelle transfer of other cellular lipids, thereby promoting normal lipid homeostasis within cells.

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Section: Sac1 Function In Different Intracellular Compartmentsmentioning

confidence: 99%

Section: Er-to-golgi Shuttling Of Sac1 In Mammalian Cells Is Controllmentioning

confidence: 99%

Sac1, a lipid phosphatase at the interface of vesicular and nonvesicular transport

Bel

Brill

2018

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“…Breast cancer cells have almost unlimited ability of survival with fast proliferation and invasion [2]. The Golgi apparatus, an organelle involved in post translational modification and sorting of proteins, is increasingly viewed as a platform for the spatial regulation of signaling molecules [3], and its function in directly regulating cancer genesis and development is widely accepted. The disassembly of Golgi was found in advanced androgen-refractory prostate cancer cells and primary prostate tumors and correlated with Gleason score and metastasis [4].…”

Section: Introductionmentioning

confidence: 99%

ATF-3/miR-590/GOLPH3 signaling pathway regulates proliferation of breast cancer

et al. 2018

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“…We recently used fluorescence resonance energy transfer (FRET) microscopy to show that Cdc42 is active at the Golgi and that this pool is important for cell polarization. 9 The Golgi apparatus is increasingly viewed as a platform for the spatial regulation of signaling molecules 10,11 and its role in cell migration and related processes such as metastasis is becoming increasingly evident. 12 We showed that the Golgi-matrix protein GM130, regulates Cdc42 specifically at the Golgi without affecting plasma membrane Cdc42.…”

Section: Introductionmentioning

confidence: 99%

Loss of GM130 in breast cancer cells and its effects on cell migration, invasion and polarity

et al. 2015

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Spatially distinct pools of the small GTPase Cdc42 were observed, but the major focus of research so far has been to investigate its signaling at the plasma membrane. We recently showed that the Golgi pool of Cdc42 is relevant for cell polarity and that it is regulated by GM130, a Golgi matrix protein. Loss of GM130 abrogated cell polarity and consistent with the notion that polarity is frequently impaired in cancer, we found that GM130 is downregulated in colorectal cancer. Whether the loss of GM130 solely affects polarity, or whether it affects other processes relevant for tumorigenesis remains unclear. In a panel of breast cancer cells lines, we investigated the consequences of GM130 depletion on traits of relevance for tumor progression, such as survival, proliferation, adhesion, migration and invasion. We show that cellular assays that depend on polarity, such as chemotaxis and wound scratch assays, are only of limited use to investigate the role of polarity modulators in cancer. Depletion of GM130 increases cellular velocity and increases the invasiveness of breast cancer cells, therefore supporting the view that alterations of polarity contribute to tumor progression.

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Regulation of protein trafficking: JNK3 at the Golgi complex

Cited by 7 publications

References 7 publications

Sac1, a lipid phosphatase at the interface of vesicular and nonvesicular transport

Sac1, a lipid phosphatase at the interface of vesicular and nonvesicular transport

ATF-3/miR-590/GOLPH3 signaling pathway regulates proliferation of breast cancer

Loss of GM130 in breast cancer cells and its effects on cell migration, invasion and polarity

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