RASSF4: Regulator of plasma membrane PI(4,5)P2

Dickson, Eamonn J.

doi:10.1083/jcb.201706042

Cited by 8 publications

(12 citation statements)

References 12 publications

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“…At ER-PM contact sites, RASSF4 acts in concert with ARF6, the upstream regulator of type I phosphatidylinositol phosphokinase (PIP5K), to regulate PI(4,5)P2 levels on the PM (Chen et al, 2017 ). Since PI(4,5)P2 is essential to position STIM1 and E-Syts, RASSF4 participates in the regulation of SOCE and ER-PM junctions indirectly through the regulation of PI(4,5)P2 homeostasis (Dickson, 2017 ).…”

Section: Regulation Of Ca 2+ Dynamics At Er-pm Conmentioning

confidence: 99%

“…Nir2 binds and transfers PA from the PM to the ER (Kim et al, 2015 ). In turn, it moves PI from the ER to the PM and generates PI(4)P and PI(4,5)P2, in which step RASSF4 and ARF6 participate (Stathopulos et al, 2006 ; Chen et al, 2017 ; Dickson, 2017 ). PI(4,5)P2 reinforces relocations of E-Syts and STIM1 at the contact sites and further regulates Ca 2+ dynamics.…”

Section: Lipid Exchanges At Er-pm Contact Sitesmentioning

confidence: 99%

“…The consumption of excess PI(4,5)P2 generates DAG and PA, which facilitate Nir2 enter the next circle. Overall, this network combines SOCE regulators with LTPs to develop a synergistic effect between Ca 2+ signaling and PI(4,5)P2 metabolism at the ER-PM junctions and extend the duration of signal transductions (Dickson, 2017 ; Ong and Ambudkar, 2020 ).…”

Section: Lipid Exchanges At Er-pm Contact Sitesmentioning

confidence: 99%

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Endoplasmic Reticulum–Plasma Membrane Contact Sites: Regulators, Mechanisms, and Physiological Functions

Qian

et al. 2021

Front. Cell Dev. Biol.

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The endoplasmic reticulum (ER) forms direct membrane contact sites with the plasma membrane (PM) in eukaryotic cells. These ER-PM contact sites play essential roles in lipid homeostasis, ion dynamics, and cell signaling, which are carried out by protein-protein or protein-lipid interactions. Distinct tethering factors dynamically control the architecture of ER-PM junctions in response to intracellular signals or external stimuli. The physiological roles of ER-PM contact sites are dependent on a variety of regulators that individually or cooperatively perform functions in diverse cellular processes. This review focuses on proteins functioning at ER-PM contact sites and highlights the recent progress in their mechanisms and physiological roles.

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Section: Regulation Of Ca 2+ Dynamics At Er-pm Conmentioning

confidence: 99%

Section: Lipid Exchanges At Er-pm Contact Sitesmentioning

confidence: 99%

Section: Lipid Exchanges At Er-pm Contact Sitesmentioning

confidence: 99%

See 1 more Smart Citation

Endoplasmic Reticulum–Plasma Membrane Contact Sites: Regulators, Mechanisms, and Physiological Functions

Qian

et al. 2021

Front. Cell Dev. Biol.

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“…PIP 2 levels in the plasma membrane are regulated by several proteins, which have been also shown to influence STIM1-Orai1 activation. These include septins, E-Syt1, Nir2, and RASSF4 [ 372 , 373 , 374 , 375 , 376 , 377 ]. Septins represent GTP-binding proteins in the plasma membrane that bind PIP 2 .…”

Section: Individual and Collective Modulation Of Ca 2+ mentioning

confidence: 99%

“…Both E-Syt1 and Nir2 are co-localized with STIM1 within these junctions to prime the cell for additional stimulation. A regulatory protein RASSF4 has been shown to control the steady-state PIP 2 levels in the plasma membrane, thus, controlling ER-PM junctions and the activation of STIM1-Orai1 [ 374 , 375 ].…”

Section: Individual and Collective Modulation Of Ca 2+ mentioning

confidence: 99%

Molecular Choreography and Structure of Ca2+ Release-Activated Ca2+ (CRAC) and KCa2+ Channels and Their Relevance in Disease with Special Focus on Cancer

Tiffner

Derler

2020

Membranes

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Ca2+ ions play a variety of roles in the human body as well as within a single cell. Cellular Ca2+ signal transduction processes are governed by Ca2+ sensing and Ca2+ transporting proteins. In this review, we discuss the Ca2+ and the Ca2+-sensing ion channels with particular focus on the structure-function relationship of the Ca2+ release-activated Ca2+ (CRAC) ion channel, the Ca2+-activated K+ (KCa2+) ion channels, and their modulation via other cellular components. Moreover, we highlight their roles in healthy signaling processes as well as in disease with a special focus on cancer. As KCa2+ channels are activated via elevations of intracellular Ca2+ levels, we summarize the current knowledge on the action mechanisms of the interplay of CRAC and KCa2+ ion channels and their role in cancer cell development.

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A “Janus” face of the RASSF4 signal in cell fate

Liu

Zhou

Martínez

et al. 2021

Journal Cellular Physiology

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RASSF4 (Ras‐association domain family 4) is a protein‐coding gene, regarded as a tumor suppressor regulated by DNA methylation. However, RASSF4 acts as a “Janus” in cell fate: death and survival. This review article focuses on the regulatory mechanisms of RASSF4 on cell death and cell survival and puts forward a comprehensive analysis of the relevant signaling pathways. The participation of RASSF4 in the regulation of intracellular store‐operated Ca2+ entry also affects cell survival. Moreover, the mechanism of inducing abnormal expression of RASSF4 was summarized. We highlight recent advances in our knowledge of RASSF4 function in the development of cancer and other clinical diseases, which may provide insight into the controversial functions of RASSF4 and its potential application in disease therapy.

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RASSF4: Regulator of plasma membrane PI(4,5)P2

Abstract: Dickson highlights work from Chen et al. demonstrating that RASSF4 regulates the generation of membrane phosphoinositides and store-operated calcium entry.

Cited by 8 publications

References 12 publications

Endoplasmic Reticulum–Plasma Membrane Contact Sites: Regulators, Mechanisms, and Physiological Functions

Endoplasmic Reticulum–Plasma Membrane Contact Sites: Regulators, Mechanisms, and Physiological Functions

Molecular Choreography and Structure of Ca2+ Release-Activated Ca2+ (CRAC) and KCa2+ Channels and Their Relevance in Disease with Special Focus on Cancer

A “Janus” face of the RASSF4 signal in cell fate

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