Secretion of the mammalian Sec14p‐like phosphoinositide‐binding p45 protein

Merkulova, Maria; Huynh, Hung; Radchenko, V. V.; Saito, Kan; Липкин, В. М.; Shuvaeva, T. M.; Mustelin, Tomas

doi:10.1111/j.1742-4658.2005.04955.x

Cited by 15 publications

(14 citation statements)

References 49 publications

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“…Moreover, COS-1 cells transduced with a Sec14l3 expression vector similarly excrete the Sec14l3 protein into the culture medium [26]. Consistent with these data, our previous proteomic experiments using rat bronchoalveolar lavage (BAL) fluids identified the Sec14l3 protein as a component of BAL fluid [16].…”

Section: Discussionmentioning

confidence: 55%

Sec14l3 Is Specifically Expressed in Mouse Airway Ciliated Cells

et al. 2011

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Airway epithelium is a key component for airway integrity. Previously, we found that expression of the Sec14l3 gene that encodes a 45-kDa secretory protein is inversely associated with the progression of experimentally induced airway inflammation and degeneration/necrosis of alveolar epithelium. In this report, using in situ hybridization we demonstrated that the ciliated cells in mouse lung selectively express Sec14l3 mRNA. In a three-dimensional culture of mouse tracheal epithelial cells, levels of the Sec14l3 mRNA correlated with the differentiation of ciliated cells. Intranasal infection of adult mice with influenza virus resulted in a 20-fold, progressive decrease in Sec14l3 mRNA expression over 10 days post infection. These results enhance the potential value of Sec14l3 as a ciliated epithelial cell-specific biomarker for the progression of airway inflammations such as airway viral infection and asthma.

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Section: Discussionmentioning

confidence: 55%

Sec14l3 Is Specifically Expressed in Mouse Airway Ciliated Cells

et al. 2011

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“…QIAquick Gel Extraction Kit, QIAquick PCR purification kit, and Ni-NTA-Agarose beads were from QIAGEN (Valencia, CA). Primer Kit II, the plasmid pET28a(+) and E. coli BL21 (DE3) cells were from Stratagene (La Jolla, CA); the plasmid pEF3HA was designed in our laboratory [6]. Phosphotyrosine and phosphothreonine were obtained from Sigma-Aldrich (St. Louis, MO) and phosphoserine from PM Biochemicals (Solon, OH).…”

Section: Methodsmentioning

confidence: 99%

Identification and characterization of DUSP27, a novel dual‐specific protein phosphatase

Friedberg¹,

Nika²,

Tautz³

et al. 2007

FEBS Letters

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A novel human dual-specific protein phosphatase (DSP), designated DUSP27, is here described. The DUSP27 gene contains three exons, rather than the predicted 4-14 exons, and encodes a 220 amino acid protein. DUSP27 is structurally similar to other small DSPs, like VHR and DUSP13. The location of DUSP27 on chromosome 10q22, 50 kb upstream of DUSP13, suggests that these two genes arose by gene duplication. DUSP27 is an active enzyme, and its kinetic parameters and were determined. DUSP27 is a cytosolic enzyme, expressed in skeletal muscle, liver and adipose tissue, suggesting its possible role in energy metabolism.

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“…All these proteins contain a GOLD domain, which is presumed to act as a protein-protein interaction module involved in Golgi function or trafficking. Unlike SEC14L2, SEC14L3 binds a different set of lipid ligands most preferentially PIP 3 and colocalizes with this lipid in the secretory vesicles [107]. The linkage of Sec14 domain with GOLD suggests roles in the integration of lipid metabolism and signaling with downstream protein complexes in organelle homeostasis or traffic.…”

Section: Mammalian Sec14-like Proteinsmentioning

confidence: 99%

Phosphatidylinositol transfer proteins: Negotiating the regulatory interface between lipid metabolism and lipid signaling in diverse cellular processes

Ghosh

Bankaitis

2011

BioFactors

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Phosphoinositides represent only a small percentage of the total cellular lipid pool. Yet, these molecules play crucial roles in diverse intracellular processes such as signal transduction at membrane-cytosol interface, regulation of membrane trafficking, cytoskeleton organization, nuclear events, and the permeability and transport functions of the membrane. A central principle in such lipid-mediated signaling is the appropriate coordination of these events. Such an intricate coordination demands fine spatial and temporal control of lipid metabolism and organization, and consistent mechanisms for specifically coupling these parameters to dedicated physiological processes. In that regard, recent studies have identified Sec14-like phosphatidylcholine transfer protein (PITPs) as "coincidence detectors," which spatially and temporally link the diverse aspects of the cellular lipid metabolome with phosphoinositide signaling. The integral role of PITPs in eukaryotic signal transduction design is amply demonstrated by the mammalian diseases associated with the derangements in the function of these proteins, to stress response and developmental regulation in plants, to fungal dimorphism and pathogenicity, to membrane trafficking in yeast, and higher eukaryotes. This review updates the recent advances made in the understanding of how these proteins, specifically PITPs of the Sec14-protein superfamily, operate at the molecular level and further describes how this knowledge has advanced our perception on the diverse biological functions of PITPs.

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Secretion of the mammalian Sec14p‐like phosphoinositide‐binding p45 protein

Cited by 15 publications

References 49 publications

Sec14l3 Is Specifically Expressed in Mouse Airway Ciliated Cells

Sec14l3 Is Specifically Expressed in Mouse Airway Ciliated Cells

Identification and characterization of DUSP27, a novel dual‐specific protein phosphatase

Phosphatidylinositol transfer proteins: Negotiating the regulatory interface between lipid metabolism and lipid signaling in diverse cellular processes

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