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Exocytosis is a form of active transport and bulk transport in which a cell transports molecules out of the cell. As an active transport mechanism, exocytosis requires the use of energy to transport material. Exocytosis and its counterpart, endocytosis, are used by all cells because most chemical substances important to them are large polar molecules that cannot pass through the hydrophobic portion of the cell membrane by passive means. Exocytosis is the process by which a large amount of molecules are released; thus it is a form of bulk transport. Exocytosis occurs via secretory portals at the cell plasma membrane called porosomes. Porosomes are permanent cup-shaped lipoprotein structure at the cell plasma membrane, where secretory vesicles transiently dock and fuse to release intra-vesicular contents from the cell.
Clusterin is a 75-80 kDa disulfide-linked heterodimeric protein associated with the clearance of cellular debris and apoptosis. In humans, clusterin is encoded by the CLU gene on chromosome 8. CLU is a molecular chaperone responsible for aiding protein folding of secreted proteins, and its three isoforms have been differentially implicated in pro- or antiapoptotic processes. Through this function, CLU is involved in many diseases related to oxidative stress, including neurodegenerative diseases, cancers, inflammatory diseases, and aging.
The exocyst is an octameric protein complex involved in vesicle trafficking, specifically the tethering and spatial targeting of post-Golgi vesicles to the plasma membrane prior to vesicle fusion. It is implicated in a number of cell processes, including exocytosis, cell migration, and growth.
Angiomotin (AMOT) is a protein that in humans is encoded by the AMOT gene. It belongs to the motin family of angiostatin binding proteins, which includes angiomotin, angiomotin-like 1 (AMOTL1) and angiomotin-like 2 (AMOTL2) characterized by coiled-coil domains at N-terminus and consensus PDZ-binding domain at the C-terminus. Angiomotin is expressed predominantly in endothelial cells of capillaries as well as angiogenic tissues such as placenta and solid tumor.
IKBKAP is a human gene encoding the IKAP protein, which is ubiquitously expressed at varying levels in all tissue types, including brain cells. The IKAP protein is thought to participate as a sub-unit in the assembly of a six-protein putative human holo-Elongator complex, which allows for transcriptional elongation by RNA polymerase II. Further evidence has implicated the IKAP protein as being critical in neuronal development, and directs that decreased expression of IKAP in certain cell types is the molecular basis for the severe, neurodevelopmental disorder familial dysautonomia. Other pathways that have been connected to IKAP protein function in a variety of organisms include tRNA modification, cell motility, and cytosolic stress signalling. Homologs of the IKBKAP gene have been identified in multiple other Eukaryotic model organisms. Notable homologs include Elp1 in yeast, Ikbkap in mice, and D-elp1 in fruit flies. The fruit fly homolog (D-elp1) has RNA-dependent RNA polymerase activity and is involved in RNA interference.
Synaptosomal-Associated Protein, 25kDa (SNAP-25) is a Target Soluble NSF (N-ethylmaleimide-sensitive factor) Attachment Protein Receptor (t-SNARE) protein encoded by the SNAP25 gene found on chromosome 20p12.2 in humans. SNAP-25 is a component of the trans-SNARE complex, which accounts for membrane fusion specificity and directly executes fusion by forming a tight complex that brings the synaptic vesicle and plasma membranes together.
Presenilins are a family of related multi-pass transmembrane proteins which constitute the catalytic subunits of the gamma-secretase intramembrane protease protein complex. They were first identified in screens for mutations causing early onset forms of familial Alzheimer's disease by Peter St George-Hyslop. Vertebrates have two presenilin genes, called PSEN1 that codes for presenilin 1 (PS-1) and PSEN2 that codes for presenilin 2 (PS-2). Both genes show conservation between species, with little difference between rat and human presenilins. The nematode worm C. elegans has two genes that resemble the presenilins and appear to be functionally similar, sel-12 and hop-1.
Histone deacetylase 2 (HDAC2) is an enzyme that in humans is encoded by the HDAC2 gene. It belongs to the histone deacetylase class of enzymes responsible for the removal of acetyl groups from lysine residues at the N-terminal region of the core histones. As such, it plays an important role in gene expression by facilitating the formation of transcription repressor complexes and for this reason is often considered an important target for cancer therapy.
Ras-related protein Ral-A (RalA) is a protein that in humans is encoded by the RALA gene on chromosome 7. This protein is one of two paralogs of the Ral protein, the other being RalB, and part of the Ras GTPase family. RalA functions as a molecular switch to activate a number of biological processes, majorly cell division and transport, via signaling pathways. Its biological role thus implicates it in many cancers.
Down syndrome critical region gene 1, also known as DSCR1, is a protein that in humans is encoded by the RCAN1 gene.
Septin 2, also known as SEPT2, is a protein which in humans is encoded by the SEPT2 gene.
Exocyst complex component 4 is a protein that in humans is encoded by the EXOC4 gene.
Exocyst complex component 2 is a protein that in humans is encoded by the EXOC2 gene.
Parkin coregulated gene protein is a protein that in humans is encoded by the PACRG gene.
Exocyst complex component 7 is a protein that in humans is encoded by the EXOC7 gene. It was formerly known as Exo70.
Exocyst complex component 3 is a protein that in humans is encoded by the EXOC3 gene.
Exocyst complex component 5 is a protein that in humans is encoded by the EXOC5 gene.
Exocyst complex component 1 is a protein that in humans is encoded by the EXOC1 gene.
Exocyst complex component 6 is a protein that in humans is encoded by the EXOC6 gene.
Ras-interacting protein 1(Rain), is a protein that in humans is encoded by the RASIP1 gene.
References
- 1 2 3 Barkefors, I; Fuchs, PF; Heldin, J; Bergström, T; Forsberg-Nilsson, K; Kreuger, J (2011). "Exocyst complex component 3-like 2 (EXOC3L2) associates with the exocyst complex and mediates directional migration of endothelial cells". The Journal of Biological Chemistry. 286 (27): 24189–99. doi: 10.1074/jbc.M110.212209 . PMC 3129200 . PMID 21566143.
- ↑ EntrezGene 90332
- ↑ Olgiati, P; Politis, AM; Papadimitriou, GN; De Ronchi, D; Serretti, A (2011). "Genetics of late-onset Alzheimer's disease: Update from the alzgene database and analysis of shared pathways". International Journal of Alzheimer's Disease. 2011: 832379. doi: 10.4061/2011/832379 . PMC 3235576 . PMID 22191060.
- ↑ Belbin, O; Carrasquillo, MM; Crump, M; Culley, OJ; Hunter, TA; Ma, L; Bisceglio, G; Zou, F; Allen, M (2011). "Investigation of 15 of the top candidate genes for late-onset Alzheimer's disease". Human Genetics. 129 (3): 273–82. doi:10.1007/s00439-010-0924-2. PMC 3036835 . PMID 21132329.
- 1 2 3 Liu, J; Guo, W (2011). "The exocyst complex in exocytosis and cell migration". Protoplasma. 249 (3): 587–597. doi:10.1007/s00709-011-0330-1. PMID 21997494. S2CID 11946932.
- 1 2 Munson, M; Novick, P (2006). "The exocyst defrocked, a framework of rods revealed". Nature Structural & Molecular Biology. 13 (7): 577–81. doi:10.1038/nsmb1097. PMID 16826234. S2CID 26645238.
- ↑ Thapa, N; Sun, Y; Schramp, M; Choi, S; Ling, K; Anderson, RA (2012). "Phosphoinositide signaling regulates the exocyst complex and polarized integrin trafficking in directionally migrating cells". Developmental Cell. 22 (1): 116–30. doi:10.1016/j.devcel.2011.10.030. PMC 3266520 . PMID 22264730.
- ↑ Carmeliet, P; Jain, RK (2011). "Molecular mechanisms and clinical applications of angiogenesis". Nature. 473 (7347): 298–307. Bibcode:2011Natur.473..298C. doi:10.1038/nature10144. PMC 4049445 . PMID 21593862.