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Dyneins are a family of cytoskeletal motor proteins that move along microtubules in cells. They convert the chemical energy stored in ATP to mechanical work. Dynein transports various cellular cargos, provides forces and displacements important in mitosis, and drives the beat of eukaryotic cilia and flagella. All of these functions rely on dynein's ability to move towards the minus-end of the microtubules, known as retrograde transport; thus, they are called "minus-end directed motors". In contrast, most kinesin motor proteins move toward the microtubules' plus-end, in what is called anterograde transport.
CCAAT-enhancer-binding proteins is a family of transcription factors composed of six members, named from C/EBPα to C/EBPζ. They promote the expression of certain genes through interaction with their promoters. Once bound to DNA, C/EBPs can recruit so-called co-activators that in turn can open up chromatin structure or recruit basal transcription factors.
Dynactin is a 23 subunit protein complex that acts as a co-factor for the microtubule motor cytoplasmic dynein-1. It is built around a short filament of actin related protein-1 (Arp1).
A-kinase anchor protein 9 is a protein that in humans is encoded by the AKAP9 gene. AKAP9 is also known as Centrosome- and Golgi-localized protein kinase N-associated protein (CG-NAP) or AKAP350 or AKAP450
Kinectin is a protein that in humans is encoded by the KTN1 gene.
Microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 is a protein that in humans is encoded by the MACF1 gene.
Structural maintenance of chromosomes protein 3 (SMC3) is a protein that in humans is encoded by the SMC3 gene. SMC3 is a subunit of the Cohesin complex which mediates sister chromatid cohesion, homologous recombination and DNA looping. Cohesin is formed of SMC3, SMC1, RAD21 and either SA1 or SA2. In humans, SMC3 is present in all cohesin complexes whereas there are multiple paralogs for the other subunits.
Citron Rho-interacting kinase is an enzyme that in humans is encoded by the CIT gene.
VAMP-Associated Protein A is a protein that in humans is encoded by the VAPA gene. Together with VAPB and VAPC it forms the VAP protein family. They are integral endoplasmic reticulum membrane proteins of the type II and are ubiquitous among eukaryotes.
Oxysterol-binding protein 1 is a protein that in humans is encoded by the OSBP gene.
Protein Hook homolog 1 is a protein that in humans is encoded by the HOOK1 gene.
Microtubule-associated protein 6 (MAP6) or stable tubule-only polypeptide is a protein that in humans is encoded by the MAP6 gene.
Protein Hook homolog 3 is a protein that in humans is encoded by the HOOK3 gene.
Coronin is an actin binding protein which also interacts with microtubules and in some cell types is associated with phagocytosis. Coronin proteins are expressed in a large number of eukaryotic organisms from yeast to humans.
Kinesin-like protein KIF1A, also known as axonal transporter of synaptic vesicles or microtubule-based motor KIF1A, is a protein that in humans is encoded by the KIF1A gene.
Protein Hook homolog 2 (HK2) is a protein that in humans is encoded by the HOOK2 gene.
Soluble N-ethylmaleimide-Sensitive Factor Attachment Proteins are a family of cytosolic adaptor proteins involved in vesicular fusion at membranes during intracellular transport and exocytosis. SNAPs interact with proteins of the SNARE complex and NSF to play a key role in recycling the components of the fusion complex. SNAPs are involved in the priming of the vesicle fusion complex during assembly, as well as in the disassembly following a vesicle fusion event. Following membrane fusion, the tethering SNARE proteins complex disassembles in response to steric changes originating from the ATPase NSF. The energy provided by NSF is transferred throughout the SNARE complex and SNAP, allowing the proteins to untangle, and recycled for future fusion events. Mammals have three SNAP genes: α-SNAP, β-SNAP, and γ-SNAP. α- and γ-SNAP are expressed throughout the body, while β-SNAP is specific to the brain. The yeast homolog of the human SNAP is Sec17, the structural diagram of which is included on this page.
The Golgi matrix is a collection of proteins involved in the structure and function of the Golgi apparatus. The matrix was first isolated in 1994 as an amorphous collection of 12 proteins that remained associated together in the presence of detergent and 150 mM NaCl. Treatment with a protease enzyme removed the matrix, which confirmed the importance of proteins for the matrix structure. Modern freeze etch electron microscopy (EM) clearly shows a mesh connecting Golgi cisternae and associated vesicles. Further support for the existence of a matrix comes from EM images showing that ribosomes are excluded from regions between and near Golgi cisternae.
Coiled-coil domain-containing protein 181 (CCDC181) is a protein that in human is encoded by C1orf114, which is located at the Chromosome 1 at 1q24.2. The accession is Q5T1D7. Researches have recently revealed that CCDC 181 is a microtubule-binding protein that interacts with murine Hook1 in haploid male germ cells and localizes to the sperm tail and motile cilia. The disruption of Hook1 may lead to inappropriate function of spermatogenesis. The dysfunction may be related to the abnormal head shape of sperm or distinctive structural changes in flagella in sperm, which can result in male infertility. An increased rate of my gene has found in the haploid phase of male cell during meiosis, thus it is believed to relate to sperm cell and aid in spermatogenesis.
Coiled-coil domain containing 88B is a protein that in humans is encoded by the CCDC88B gene.
References
- ↑ Kramer H, Liu X, Walenta JH, Didier AJ (2001). "The Golgi-associated hook3 protein is a member of a novel family of microtubule-binding proteins". J. Cell Biol. 152 (5): 923–934. doi:10.1083/jcb.152.5.923. PMC 2198811 . PMID 11238449.
- ↑ Engel W, Dixkens C, Neesen J, Burfeind P, Mendoza-lujambio I, Meinhardt A, Hoyer-fender S (2002). "The Hook1 gene is non-functional in the abnormal spermatozoon head shape (azh) mutant mouse". Hum. Mol. Genet. 11 (14): 1647–1658. doi: 10.1093/hmg/11.14.1647 . PMID 12075009.
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