instruction:
In this task, you're given a paragraph and title from the research paper. Your task is to classify whether the given title is suitable or not for the research paper based on the given paragraph. Return "True" if title is proper according to paragraph else "False".
question:
Paragraph: Recent results have provided increasing evidence for the existence of an intermediate membrane compartment between the rough endoplasmic reticulum and the Golgi complex which seems to function in protein sorting and the regulation of membrane traffic in the early part of the exocytic pathway . Localization of resident marker proteins has shown that this compartment consists of both peripheral and central elements . The aim of the present review is to combine the data on the pre-Golgi compartment with previous ideas of membrane traffic at the ER-Golgi interface . We propose a model which describes how mobile, endosome-like elements of the pre-Golgi compartment function in the generation of the compositional andfunctional boundary between the widely distributed ER and the more central4 located Golgi stacks . 
 Title: Pathways of protein sorting and membrane traffic between the rough endoplasmic reticulum and the Golgi complex jaakko Saraste *t and Esa Kuismanent
answer:
True


question:
Paragraph: The yeast Kre2p/Mntlp cxl,2-mannosyltransferase is a type II membrane protein with a short cytoplasmic amino terminus, a membrane-spanning region, and a large catalytic luminal domain containing one N-glycosylation site. Anti-Kre2p/Mntlp antibodies identify a 60-kD integral membrane protein that is progressively N-glycosylated in an MNNl-dependent manner. Kre2p/Mntlp is localized in a Golgi compartment that overlaps with that containing the medial-Golgi mannosyltransferase Mnnlp, and distinct from that including the late Golgi protein Kexlp. To determine which regions of Kre2p/Mntlp are required for Golgi localization, Kre2p/Mntlp mutant proteins were assem-bled by substitution of Kre2p domains with equivalent sequences from the vacuolar proteins DPAP B and Pho8p. Chimeric proteins were tested for correct topology, in vitro and in vivo activity, and were localized intracellularly by indirect immunofluorescence. The resuits demonstrate that the NH2-terminal cytoplasmic domain is necessary for correct Kre2p Golgi localization whereas, the membrane-spanning and stem domains are dispensable. However, in a test of targeting sufficiency, the presence of the entire Kre2p cytoplasmic tail, plus the transmembrane domain and a 36-amino acid residue luminal stem region was required to localize a Pho8p reporter protein to the yeast Golgi. T HE Golgi apparatus plays a fundamental role in glycan processing and sorting of newly synthesized proteins in the secretory pathway of eukaryotic cells. The Golgi apparatus of a typical mammalian cell is composed of a polarized stack of membranous saccules that are differentiated into functionally distinct subcompartments. After the addition of core N-linked sugar moieties in the endoplasmic reticulum, glycoproteins proceed through the cis-Golgi network, the cis-, medial-, and transcisternae, and the trans-Golgi network, where further modifications take place. These include the addition of O-linked sugars and the elaboration, in a protein-specific manner, of complex N-linked carbohydrate structures. The Golgi apparatus also constitutes a major organelle responsible for protein trafficking where particular proteins are directed to precise cellular locations. Two specific Golgi subcompartments have been found to be involved in protein sorting. The cis-Golgi network constitutes the site from which many resident ER proteins are retrieved, and the main function of the TGN is to direct glycoproteins exiting the Golgi complex to either the lysosome or the cell surface ( 
 Title: Localization and Targeting of the Saccharomyces cerevisiae Kre2p/Mnt lp oL 1,2-Mannosyltransferase to a medial.Gol Compartment
answer:
False


question:
Paragraph: Ebola virus (EBOV) enters host cells by macropinocytosis, a poorly understood process. Recent studies have suggested that cell factors involved in autophagy, an evolutionally conserved pathway leading to the lysosomal degradation of protein aggregates and organelles during cellular stress, also have roles in macropinocytosis. Here, we demonstrate that autophagy-associated proteins are required for trafficking of EBOV into the cell body. Depleting cells of beclin 1, autophagy-related protein 7, or microtubule-associated protein 1A/B light chain 3B (LC3B) abolished EBOV uptake, owing to a block in vesicle formation at the cell surface. Both LC3B-I and LC3B-II interacted with macropinocytic structures. Our work indicates that, although various forms of LC3B possess an inherent ability to associate with forming macropinosomes, LC3B-II is critical for internalization of macropinocytic vesicles and, therefore, EBOV from the cell surface. 
 Title: The Journal of Infectious Diseases Autophagy-Associated Proteins Control Ebola Virus Internalization Into Host Cells
answer:

True