Nexin
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Nexin
Nexin is a proteinous inter-doublet linkage that prevents microtubules in the outer layer of axonemes from moving with respect to one another; otherwise, vesicular transport proteins such as dynein would dissolve the whole structure. Page 26 See also * Sorting nexin Sorting nexins are a large group of proteins that are localized in the cytoplasm and have the potential for membrane association either through their lipid-binding PX domain (a phospholipid-binding motif) or through protein–protein inter ... References {{Authority control Proteins ...
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Sorting Nexin
Sorting nexins are a large group of proteins that are localized in the cytoplasm and have the potential for membrane association either through their lipid-binding PX domain (a phospholipid-binding motif) or through protein–protein interactions with membrane-associated protein complexes Some members of this family have been shown to facilitate protein sorting. Family members In humans, sorting nexins are transcribed from the following genes: Structure Sorting nexins either consist solely of a PX domain (e.g. SNX3) or have a modular structure made up of the PX and additional domains. A subgroup of sorting nexins (comprising, in humans, SNX1, SNX2, SNX4, SNX5, SNX6, SNX7, SNX8, SNX9, SNX18, SNX30, SNX32 and SNX33) possess a BAR domain at their C-terminus. (The BAR domain of SNXs 1, 2, 4, 7, 8 and 30 is classified by pfam as 'Vps5 C terminal like'.) An example of a sorting nexin domain structure can be seen here for SNX1: # NTD – N-terminal domain # PX d ...
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Axoneme
An axoneme, also called an axial filament is the microtubule-based cytoskeletal structure that forms the core of a cilium or flagellum. Cilia and flagella are found on many cells, organisms, and microorganisms, to provide motility. The axoneme serves as the "skeleton" of these organelles, both giving support to the structure and, in some cases, the ability to bend. Though distinctions of function and length may be made between cilia and flagella, the internal structure of the axoneme is common to both. Structure Inside a cilium and a flagellum is a microtubule-based cytoskeleton called the axoneme. The axoneme of a primary cilium typically has a ring of nine outer microtubule doublets (called a 9+0 axoneme), and the axoneme of a motile cilium has two central microtubules in addition to the nine outer doublets (called a 9+2 axoneme). The axonemal cytoskeleton acts as a scaffolding for various protein complexes and provides binding sites for molecular motor proteins s ...
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Vesicular Transport Protein
A vesicular transport protein, or vesicular transporter, is a membrane protein that regulates or facilitates the movement of specific molecules across a vesicle's membrane. As a result, vesicular transporters govern the concentration of molecules within a vesicle. Types Examples include: * Archain * ARFs * Clathrin * Caveolin * Dynamin and related proteins, such as the EHD protein family * Rab proteins * SNAREs * Vesicular transport adaptor proteins e.g. Sorting nexins * Synaptotagmin * TRAPP complex * Synaptophysin * Auxilin Pathways There are multiple pathways, each using its own coat and GTPase. * COP 1 (Cytosolic coat protein complex ) : retrograde transport; Golgi ----> Endoplasmic reticulum * COP 2 (Cytosolic coat protein complex ) : anterograde transport; RER -----> cis-Golgi * Clathrin : trans-Golgi ----> Lysosomes, Plasma membrane ----> Endosomes ( receptor-mediated endocytosis) See also * Membrane transport protein A membrane transport protein (or si ...
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Eukaryotic Flagellum
Eukaryotes () are organisms whose cells have a nucleus. All animals, plants, fungi, and many unicellular organisms, are Eukaryotes. They belong to the group of organisms Eukaryota or Eukarya, which is one of the three domains of life. Bacteria and Archaea (both prokaryotes) make up the other two domains. The eukaryotes are usually now regarded as having emerged in the Archaea or as a sister of the Asgard archaea. This implies that there are only two domains of life, Bacteria and Archaea, with eukaryotes incorporated among archaea. Eukaryotes represent a small minority of the number of organisms, but, due to their generally much larger size, their collective global biomass is estimated to be about equal to that of prokaryotes. Eukaryotes emerged approximately 2.3–1.8 billion years ago, during the Proterozoic eon, likely as flagellated phagotrophs. Their name comes from the Greek εὖ (''eu'', "well" or "good") and κάρυον (''karyon'', "nut" or "kernel"). Eu ...
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Microtubule
Microtubules are polymers of tubulin that form part of the cytoskeleton and provide structure and shape to eukaryotic cells. Microtubules can be as long as 50 micrometres, as wide as 23 to 27  nm and have an inner diameter between 11 and 15 nm. They are formed by the polymerization of a dimer of two globular proteins, alpha and beta tubulin into protofilaments that can then associate laterally to form a hollow tube, the microtubule. The most common form of a microtubule consists of 13 protofilaments in the tubular arrangement. Microtubules play an important role in a number of cellular processes. They are involved in maintaining the structure of the cell and, together with microfilaments and intermediate filaments, they form the cytoskeleton. They also make up the internal structure of cilia and flagella. They provide platforms for intracellular transport and are involved in a variety of cellular processes, including the movement of secretory vesicles, ...
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Dynein
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. Classification Dyneins can be divided into two groups: cytoplasmic dyneins and axonemal dyneins, which are also called ciliary or flagellar dyneins. * cytoplasmic ** heavy chain: DYNC1H1, DYNC2H1 ** intermediate chain: DYNC1I1, DYNC1I2 ** light intermediate chain: DYNC1LI1, DYNC1LI2, DYNC2LI1 ** light chain: DYNLL1, DYNLL2, DYNLRB1, DYNLRB2, DYNLT1, DYNLT3 * axo ...
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