Lipid transfer proteins and the tuning of compartmental identity in the Golgi apparatus

McDermott, Mark I.; Mousley, Carl J.

doi:10.1016/j.chemphyslip.2016.06.005

Cited by 8 publications

(5 citation statements)

References 390 publications

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“…Unfortunately, an alternative nomenclature also exists within the literature, which defines class I and class II PITPs by whether they are single-or multi-domain proteins, respectively. In that classification system, PITPnc1 is assigned to class I (162). In this review, we use the former definition and so describe PITPnc1 as a class II protein.…”

Section: Start-like Pitpsmentioning

confidence: 99%

The interface between phosphatidylinositol transfer protein function and phosphoinositide signaling in higher eukaryotes

Grabon

Bankaitis

McDermott

2019

Journal of Lipid Research

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P 3 ]. Yeasts (Saccharomyces) synthesize all of these except PtdIns(3,4)P 2 and PtdIns(3,4,5)P 3. This cohort of molecules is produced by a series of reversible phosphorylation and dephosphorylation reactions catalyzed by phosphoinositide kinases (PIKs) and phosphatases, respectively, that target the inositol headgroup at positions C3, C4, and C5 (1, 2). These chemically distinct lipids, although small in number, control an impressively large set of intracellular activities. How is such diversification of biological function achieved? Current views for how PtdIns and phosphoinositide signaling are diversified focus on regulatory mechanisms that include: the regulation and localization of the enzymes that produce, degrade, or sequester phosphoinositides; the identities of the effector proteins that recognize these Abstract Phosphoinositides are key regulators of a large number of diverse cellular processes that include membrane trafficking, plasma membrane receptor signaling, cell proliferation, and transcription. How a small number of chemically distinct phosphoinositide signals are functionally amplified to exert specific control over such a diverse set of biological outcomes remains incompletely understood. To this end, a novel mechanism is now taking shape, and it involves phosphatidylinositol (PtdIns) transfer proteins (PITPs). The concept that PITPs exert instructive regulation of PtdIns 4-OH kinase activities and thereby channel phosphoinositide production to specific biological outcomes, identifies PITPs as central factors in the diversification of phosphoinositide signaling. There are two evolutionarily distinct families of PITPs: the Sec14-like and the StAR-related lipid transfer domain (START)-like families. Of these two families, the START-like PITPs are the least understood. Herein, we review recent insights into the biochemical, cellular, and physiological function of both PITP families with greater emphasis on the START-like PITPs, and we discuss the underlying mechanisms through which these proteins regulate phosphoinositide signaling and how these actions translate to human health and disease.-Grabon, A., V. A. Bankaitis, and M. I. McDermott. The interface between phosphatidylinositol transfer protein function and phosphoinositide signaling in higher eukaryotes.

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Section: Start-like Pitpsmentioning

confidence: 99%

The interface between phosphatidylinositol transfer protein function and phosphoinositide signaling in higher eukaryotes

Grabon

Bankaitis

McDermott

2019

Journal of Lipid Research

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“…26 This transport pathway proceeds to Golgi cisternae, the trans-Golgi network (TGN), and then, targeting membranes beyond, such as the plasma membrane and endosomes. [26][27][28] The export of cargo proteins by the COPII vesicles from the ERES has been considered to take place in both selective and nonselective manners to process a tremendous variety of proteins. The rate of export in the nonselective mechanism called a bulk flow was estimated according to measurements of secretion of a small, soluble, protease domain of Semliki Forest virus (SFV) capsid in CHO and Madin-Darby canine kidney (MDCK) type II cells.…”

Section: Vesicular Transportmentioning

confidence: 99%

“…In the vesicular transport in mammalian cells, lipids are incorporated, along with newly synthesized proteins having correct fold, into coat protein complex II (COPII) vesicles by forming the membrane bilayers for export from the ER exist sites (ERES) to the ER‐Golgi intermediate compartment (ERGIC) (or vesicular tubular clusters (VTCs) in other words) 26 . This transport pathway proceeds to Golgi cisternae, the trans ‐Golgi network (TGN), and then, targeting membranes beyond, such as the plasma membrane and endosomes 26‐28 …”

Section: Introductionmentioning

confidence: 99%

Phosphatidylserine biosynthesis pathways in lipid homeostasis: Toward resolution of the pending central issue for decades

Kimura

2020

FASEB j.

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Enzymatic control of lipid homeostasis in the cell is a vital element in the complex organization of life. Phosphatidylserine (PS) is an essential anionic phospholipid of cell membranes, and conducts numerous roles for their structural and functional integrity. In mammalian cells, two distinct enzymes phosphatidylserine synthases-1 (PSS1) and-2 (PSS2) in the mitochondria-associated membrane (MAM) in the ER perform de novo synthesis of PS. It is based on base-exchange reactions of the preexisting dominant phospholipids phosphatidylcholine (PC) and phosphatidylethanolamine (PE). While PSS2 specifically catalyzes the reaction "PE → PS," whether or not PSS1 is responsible for the same reaction along with the reaction "PC → PS" remains unsettled despite its fundamental impact on the major stoichiometry. We propose here that a key but the only report that appeared to have put scientists on hold for decades in answering to this issue may be viewed consistently with other available research reports; PSS1 utilizes the two dominant phospholipid classes at a similar intrinsic rate. In this review, we discuss the issue in view of the current information for the enzyme machineries, membrane structure and dynamics, intracellular network of lipid transport, and PS synthesis in health and disease. Resolution of the pending issue is thus critical in advancing our understanding of roles of the essential anionic lipid in biology, health, and disease.

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“…The Golgi complex (CG) plays a central role in eukaryotic cells, serving as an intermediary and bidirectional axis of protein and lipid trafficking in the endomembrane system [107]. In the case of T. cruzi, Carvalho et al [82] described that after long infection times, there would be no change in GC distribution, remaining in the perinuclear region.…”

Section: Organelles Involved In Parasitophorous Vacuole Formationmentioning

confidence: 99%

How Does the Main Infective Stage ofT. cruziEnter and Avoid Degradation in Host Cells? A Description of the Pathways and Organelles Involved on These Processes

Barrias¹,

Reignault²,

Souza³

2019

Biology OfTrypanosoma Cruzi

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Trypanosoma cruzi, the etiological agent of Chagas disease, is an intracellular parasite that targets specific proteins of the host cell resulting in the generation of a unique parasitophorous vacuole (PV). As an intracellular parasite, T. cruzi interacts with cells from the mammalian host. Here we review aspects related with the binding of the main infective developmental stage (trypomastigote) to the host cell and its recognition by surface-exposed ligands/receptors. This process involves numerous signaling pathways and culminates in the entry of the parasite and modifications in both cells. The invasion of trypomastigotes occurs through multiple endocytic process, assembly of the PV, interaction of this vacuole with the endolysosomal system, lysis of the PV membrane, and multiplication of amastigotes within the cell in direct contact with host cell organelles.assumed that replicating epimastigotes present in the insect gut are not infective to mammalian host. During the vector infection (caused by a hematophagous insect of the family Reduviidae), metacyclic trypomastigotes [8], which penetrate the vertebrate host (several mammals, including man), are released along with their excreta coming in contact with conjunctiva areas or through small lesions in the own site of the bite (favored by the itch caused after the insect's bite). In turn, metacyclic trypomastigotes are able to invade virtually all cell types in the vertebrate host, especially muscle cells, fibroblasts, and macrophages [6]. At this moment, the intracellular cycle of T. cruzi begins, where the firing of several signaling cascades culminates with the closure of the parasitophorous vacuole (PV) where the parasite is found [9,10]. After the PV closure, the process of differentiation of the parasite from the trypomastigote stage to the amastigote stage begins. At the same time, fragmentation of the PV membrane takes place most probably due to the increased concentration of the Tc-Tox perforin-like protein produced by the parasite [11]. After the destruction of the vacuole, the parasite, in the process of differentiation, will be found in the cytoplasm of the host cell where it will initiate its multiplication and subsequent differentiation for trypomastigotes culminating in the rupture of the host cell (Figure 1) [13]. The whole process of formation of the parasitophorous vacuole until its rupture counts on the participation of several organelles of the host cell. Among these, the best characterized is the participation of host cell endosomes and lysosomes. It is the fusion of these organelles with the PV membrane that probably allows the increase or expansion of the PV. In addition, this process is also responsible for the generation of an acidic environment within the PV, which probably will potentiate the action of Tc-Tox and PV membrane fragmentation [13]. Wilkowsky and colleagues [14] have shown that early and late endosomes were critical for vacuole formation. In addition, other organelles responsible for the production of proteins and energy (...

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Lipid transfer proteins and the tuning of compartmental identity in the Golgi apparatus

Cited by 8 publications

References 390 publications

The interface between phosphatidylinositol transfer protein function and phosphoinositide signaling in higher eukaryotes

The interface between phosphatidylinositol transfer protein function and phosphoinositide signaling in higher eukaryotes

Phosphatidylserine biosynthesis pathways in lipid homeostasis: Toward resolution of the pending central issue for decades

How Does the Main Infective Stage ofT. cruziEnter and Avoid Degradation in Host Cells? A Description of the Pathways and Organelles Involved on These Processes

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