SMP domain proteins in membrane lipid dynamics

Jeyasimman, Darshini; Saheki, Yasunori

doi:10.1016/j.bbalip.2019.04.007

Cited by 22 publications

(22 citation statements)

References 76 publications

(130 reference statements)

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“…Tricalbins are homologs of mammalian extended-synaptotagmins (E-Syts), which belong to the synaptotagmin-like mitochondrial lipid-binding protein (SMP) domain protein family (21)(22)(23)(24). All tricalbins are anchored to the ER membrane through their N-terminal hydrophobic domain, followed by an SMP domain and multiple C2 domains.…”

Section: J O U R N a L P R E -P R O O Fmentioning

confidence: 99%

“…The ER-PM MCSs are essential for calcium homeostasis, lipid metabolism, and signal transduction, which are mediated by diverse functional proteins (2)(3)(4)(5). Lipid transfer proteins (LTPs) sense and transport lipids between the membranes and play central roles at ER-PM MCSs (6)(7)(8)(9)(10). Most of the LTPs span and tether two opposed membranes when they perform lipid exchange, highlighting the essential roles of LTPs in maintaining the architectures of MCSs.…”

Section: Introductionmentioning

confidence: 99%

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Calcium-dependent and -independent lipid transfer mediated by tricalbins in yeast

Qian

et al. 2021

Journal of Biological Chemistry

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Section: J O U R N a L P R E -P R O O Fmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Calcium-dependent and -independent lipid transfer mediated by tricalbins in yeast

Qian

et al. 2021

Journal of Biological Chemistry

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“…The ER extends throughout the cytoplasm, forming physical contacts with virtually all other cellular organelles and the PM (Phillips and Voeltz, 2016; Wu et al, 2018). Growing evidence indicates that these membrane contact sites play critical roles in cellular physiology, including lipid exchange and delivery via non-vesicular lipid transport that is facilitated by lipid transfer proteins (LTPs) (Antonny et al, 2018; Drin, 2014; Elbaz and Schuldiner, 2011; Holthuis and Menon, 2014; Jeyasimman and Saheki, 2019; Kumar et al, 2018; Lahiri et al, 2015; Lev, 2012; Luo et al, 2019; Nishimura and Stefan, 2019; Petrungaro and Kornmann, 2019; Saheki et al, 2016; Saheki and De Camilli, 2017a; Saheki and De Camilli, 2017b; Wong et al, 2018). Thus, LTPs may participate in intracellular cholesterol transport and may help to maintain PM cholesterol homeostasis by regulating non-vesicular cholesterol transport between the PM and the ER at ER–PM contact sites.…”

Section: Introductionmentioning

confidence: 99%

Movement of accessible plasma membrane cholesterol by the GRAMD1 lipid transfer protein complex

Naito

Ercan

Krshnan

et al. 2019

eLife

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Cholesterol is a major structural component of the plasma membrane (PM). The majority of PM cholesterol forms complexes with other PM lipids, making it inaccessible for intracellular transport. Transition of PM cholesterol between accessible and inaccessible pools maintains cellular homeostasis, but how cells monitor the accessibility of PM cholesterol remains unclear. We show that endoplasmic reticulum (ER)-anchored lipid transfer proteins, the GRAMD1s, sense and transport accessible PM cholesterol to the ER. GRAMD1s bind to one another and populate ER-PM contacts by sensing a transient expansion of the accessible pool of PM cholesterol via their GRAM domains. They then facilitate the transport of this cholesterol via their StART-like domains. Cells that lack all three GRAMD1s exhibit striking expansion of the accessible pool of PM cholesterol as a result of less efficient PM to ER transport of accessible cholesterol. Thus, GRAMD1s facilitate the movement of accessible PM cholesterol to the ER in order to counteract an acute increase of PM cholesterol, thereby activating non-vesicular cholesterol transport.

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“…The ER extends throughout the cytoplasm, forming physical contacts with virtually all other cellular compartments, including the PM (Phillips & Voeltz, 2016;Wu et al, 2018). These membrane contact sites play critical roles in many aspects of cell physiology, including the non-vesicular exchange/delivery of specific lipids (e.g., cholesterol) by lipid transfer proteins (Elbaz & Schuldiner, 2011;Lev, 2012;Drin, 2014;Holthuis & Menon, 2014;Gatta et al, 2015;Murley et al, 2015;Saheki et al, 2016;Saheki & De Camilli, 2017a,b;Antonny et al, 2018;Luo et al, 2018;Jeyasimman & Saheki, 2019;Nishimura & Stefan, 2019;Petrungaro & Kornmann, 2019;Wong et al, 2019;Lees & Reinisch, 2020;Meng et al, 2020;Prinz et al, 2020). We and others recently found that a family of evolutionarily conserved and ER-anchored sterol transfer proteins, the GRAMD1s/Asters (GRAMD1a/Aster-A, GRAMD1b/Aster-B, and GRAMD1c/Aster-C) (the Lam/Ltc proteins in yeast), mediate nonvesicular sterol transport from the PM to the ER at ER-PM contact sites, thereby contributing to sterol homeostasis (Gatta et al, 2015;Sandhu et al, 2018;Naito et al, 2019;Marek et al, 2020).…”

Section: Introductionmentioning

confidence: 99%

Molecular basis of accessible plasma membrane cholesterol recognition by the GRAM domain of GRAMD1b

et al. 2021

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Cholesterol is essential for cell physiology. Transport of the "accessible" pool of cholesterol from the plasma membrane (PM) to the endoplasmic reticulum (ER) by ER-localized GRAMD1 proteins (GRAMD1a/1b/1c) contributes to cholesterol homeostasis. However, how cells detect accessible cholesterol within the PM remains unclear. We show that the GRAM domain of GRAMD1b, a coincidence detector for anionic lipids, including phosphatidylserine (PS), and cholesterol, possesses distinct but synergistic sites for sensing accessible cholesterol and anionic lipids. We find that a mutation within the GRAM domain of GRAMD1b that is associated with intellectual disability in humans specifically impairs cholesterol sensing. In addition, we identified another point mutation within this domain that enhances cholesterol sensitivity without altering its PS sensitivity. Cell-free reconstitution and cell-based assays revealed that the ability of the GRAM domain to sense accessible cholesterol regulates membrane tethering and determines the rate of cholesterol transport by GRAMD1b. Thus, cells detect the codistribution of accessible cholesterol and anionic lipids in the PM and fine-tune the non-vesicular transport of PM cholesterol to the ER via GRAMD1s.

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SMP domain proteins in membrane lipid dynamics

Cited by 22 publications

References 76 publications

Calcium-dependent and -independent lipid transfer mediated by tricalbins in yeast

Calcium-dependent and -independent lipid transfer mediated by tricalbins in yeast

Movement of accessible plasma membrane cholesterol by the GRAMD1 lipid transfer protein complex

Molecular basis of accessible plasma membrane cholesterol recognition by the GRAM domain of GRAMD1b

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