PMC:4621299 / 1522-3503 JSONTXT

{"project":"TEST0","denotations":[{"id":"26578865-226-234-323807","span":{"begin":240,"end":244},"obj":"[\"21112967\"]"},{"id":"26578865-233-241-323808","span":{"begin":264,"end":268},"obj":"[\"22300173\"]"},{"id":"26578865-110-118-323810","span":{"begin":404,"end":408},"obj":"[\"15932880\"]"},{"id":"26578865-130-138-323811","span":{"begin":424,"end":428},"obj":"[\"16020545\"]"},{"id":"26578865-232-240-323812","span":{"begin":896,"end":900},"obj":"[\"9875843\"]"},{"id":"26578865-223-231-323813","span":{"begin":1469,"end":1473},"obj":"[\"14744428\"]"},{"id":"26578865-234-242-323814","span":{"begin":1952,"end":1956},"obj":"[\"22160157\"]"}],"text":"The Conserved Oligomeric Golgi (COG) complex is an evolutionarily conserved hetero-octameric protein complex that is a proposed membrane tether during vesicular trafficking at the Golgi apparatus (Lupashin and Ungar, 2008; Reynders et al., 2011; Miller and Ungar, 2012; Willett et al., 2013b). COG is composed of two functionally distinct sub-complexes lobe A (COG1-4) and lobe B (COG5-8) (Fotso et al., 2005; Ungar et al., 2005). Secretory and transmembrane proteins make up 30–50% of all cellular proteins, and are trafficked through the endoplasmic reticulum (ER) to the Golgi for folding and modifications before delivery to their final destination. Secretory cargo molecules are thought to travel through the Golgi complex mostly inside flat cisternae that are constantly maturing in a cis-to-trans (anterograde) fashion via the so called cisternal maturation mechanism (Glick and Malhotra, 1998). However, resident Golgi proteins and Soluble NSF Attachment protein Receptors (SNAREs) are constantly recycled back in vesicular carriers to replenish the content of newly formed cis-cisternae. COG regulates the recycling of vesicles containing glycosylation enzymes and other resident Golgi proteins in a trans-to-cis (retrograde) direction. An intricate assortment of trafficking machineries including small Rab-GTPases, SNAREs, Sec1/Munc18 (SM) proteins, vesicular coat proteins, and tethering proteins are required for vesicular transport (Bonifacino and Glick, 2004). Intracellular pathways rely on these protein families at each step of vesicular transport. Though the functional interaction between the tethers and other trafficking regulators is not completely understood, a multi-subunit tethering complex (MTC), like the COG complex, may coordinate the interactions between all other components of the trafficking machinery at the site of vesicle docking on the target membrane for efficient fusion of the two membranes (Cottam and Ungar, 2012; Willett et al., 2013b)."}

{"project":"0_colil","denotations":[{"id":"26578865-21112967-323807","span":{"begin":240,"end":244},"obj":"21112967"},{"id":"26578865-22300173-323808","span":{"begin":264,"end":268},"obj":"22300173"},{"id":"26578865-15932880-323810","span":{"begin":404,"end":408},"obj":"15932880"},{"id":"26578865-16020545-323811","span":{"begin":424,"end":428},"obj":"16020545"},{"id":"26578865-9875843-323812","span":{"begin":896,"end":900},"obj":"9875843"},{"id":"26578865-14744428-323813","span":{"begin":1469,"end":1473},"obj":"14744428"},{"id":"26578865-22160157-323814","span":{"begin":1952,"end":1956},"obj":"22160157"}],"text":"The Conserved Oligomeric Golgi (COG) complex is an evolutionarily conserved hetero-octameric protein complex that is a proposed membrane tether during vesicular trafficking at the Golgi apparatus (Lupashin and Ungar, 2008; Reynders et al., 2011; Miller and Ungar, 2012; Willett et al., 2013b). COG is composed of two functionally distinct sub-complexes lobe A (COG1-4) and lobe B (COG5-8) (Fotso et al., 2005; Ungar et al., 2005). Secretory and transmembrane proteins make up 30–50% of all cellular proteins, and are trafficked through the endoplasmic reticulum (ER) to the Golgi for folding and modifications before delivery to their final destination. Secretory cargo molecules are thought to travel through the Golgi complex mostly inside flat cisternae that are constantly maturing in a cis-to-trans (anterograde) fashion via the so called cisternal maturation mechanism (Glick and Malhotra, 1998). However, resident Golgi proteins and Soluble NSF Attachment protein Receptors (SNAREs) are constantly recycled back in vesicular carriers to replenish the content of newly formed cis-cisternae. COG regulates the recycling of vesicles containing glycosylation enzymes and other resident Golgi proteins in a trans-to-cis (retrograde) direction. An intricate assortment of trafficking machineries including small Rab-GTPases, SNAREs, Sec1/Munc18 (SM) proteins, vesicular coat proteins, and tethering proteins are required for vesicular transport (Bonifacino and Glick, 2004). Intracellular pathways rely on these protein families at each step of vesicular transport. Though the functional interaction between the tethers and other trafficking regulators is not completely understood, a multi-subunit tethering complex (MTC), like the COG complex, may coordinate the interactions between all other components of the trafficking machinery at the site of vesicle docking on the target membrane for efficient fusion of the two membranes (Cottam and Ungar, 2012; Willett et al., 2013b)."}

{"project":"2_test","denotations":[{"id":"26578865-21112967-38257288","span":{"begin":240,"end":244},"obj":"21112967"},{"id":"26578865-22300173-38257289","span":{"begin":264,"end":268},"obj":"22300173"},{"id":"26578865-15932880-38257291","span":{"begin":404,"end":408},"obj":"15932880"},{"id":"26578865-16020545-38257292","span":{"begin":424,"end":428},"obj":"16020545"},{"id":"26578865-9875843-38257293","span":{"begin":896,"end":900},"obj":"9875843"},{"id":"26578865-14744428-38257294","span":{"begin":1469,"end":1473},"obj":"14744428"},{"id":"26578865-22160157-38257295","span":{"begin":1952,"end":1956},"obj":"22160157"}],"text":"The Conserved Oligomeric Golgi (COG) complex is an evolutionarily conserved hetero-octameric protein complex that is a proposed membrane tether during vesicular trafficking at the Golgi apparatus (Lupashin and Ungar, 2008; Reynders et al., 2011; Miller and Ungar, 2012; Willett et al., 2013b). COG is composed of two functionally distinct sub-complexes lobe A (COG1-4) and lobe B (COG5-8) (Fotso et al., 2005; Ungar et al., 2005). Secretory and transmembrane proteins make up 30–50% of all cellular proteins, and are trafficked through the endoplasmic reticulum (ER) to the Golgi for folding and modifications before delivery to their final destination. Secretory cargo molecules are thought to travel through the Golgi complex mostly inside flat cisternae that are constantly maturing in a cis-to-trans (anterograde) fashion via the so called cisternal maturation mechanism (Glick and Malhotra, 1998). However, resident Golgi proteins and Soluble NSF Attachment protein Receptors (SNAREs) are constantly recycled back in vesicular carriers to replenish the content of newly formed cis-cisternae. COG regulates the recycling of vesicles containing glycosylation enzymes and other resident Golgi proteins in a trans-to-cis (retrograde) direction. An intricate assortment of trafficking machineries including small Rab-GTPases, SNAREs, Sec1/Munc18 (SM) proteins, vesicular coat proteins, and tethering proteins are required for vesicular transport (Bonifacino and Glick, 2004). Intracellular pathways rely on these protein families at each step of vesicular transport. Though the functional interaction between the tethers and other trafficking regulators is not completely understood, a multi-subunit tethering complex (MTC), like the COG complex, may coordinate the interactions between all other components of the trafficking machinery at the site of vesicle docking on the target membrane for efficient fusion of the two membranes (Cottam and Ungar, 2012; Willett et al., 2013b)."}