Mitochondrial Fission
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Mitochondrial Fission
Mitochondrial fission is the process where mitochondria divide or segregate into two separate mitochondrial organelles. Mitochondrial fission is counteracted by the process of mitochondrial fusion, whereby two separate mitochondria can fuse together to form a large one. Mitochondrial fusion in turn can result in elongated mitochondrial networks. Both mitochondrial fission and fusion are balanced in the cell, and mutations interfering with either processes are associated with a variety of diseases. Mitochondria can divide by prokaryotic binary fission and since they require mitochondrial DNA for their function, fission is coordinated with DNA replication. Some of the proteins that are involved in mitochondrial fission have been identified and some of them are associated with mitochondrial diseases. Mitochondrial fission has significant implications in stress response and apoptosis. Mechanism FtsZ Localization The FtsZ protein (a homologue to eukaryotic tubulin), found in many bacte ...
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HeLa MtGFP
HeLa (; also Hela or hela) is an immortalized cell line used in scientific research. It is the oldest and most commonly used human cell line. The line is derived from cervical cancer cells taken on February 8, 1951, named after Henrietta Lacks, a 31-year-old African-American mother of five, who died of cancer on October 4, 1951. The cell line was found to be remarkably durable and prolific, which allows it to be used extensively in scientific study. The cells from Lacks's cancerous cervical tumor were taken without her knowledge or consent, which was common practice in the United States at the time. Cell biologist George Otto Gey found that they could be kept alive, and developed a cell line. Previously, cells cultured from other human cells would only survive for a few days. Cells from Lacks's tumor behaved differently. History Origin In 1951, a patient named Henrietta Lacks was admitted to the Johns Hopkins Hospital with symptoms of irregular vaginal bleeding, and was ...
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DNM1L
Dynamin-1-like protein is a GTPase that regulates mitochondrial fission. In humans, dynamin-1-like protein, which is typically referred to as dynamin-related protein 1 (Drp1), is encoded by the ''DNM1L'' gene and is part of the dynamin superfamily (DSP) family of proteins. Structure Drp1, which is a member of the dynamin superfamily of proteins, consists of a GTPase and GTPase effector domain that are separated from each other by a helical segment of amino acids. There are 3 mouse and 6 human isoforms of Drp1, including a brain-specific variant. Drp1 exists as homooligomers and its function relies on its oligomerization ability. Function Mitochondria routinely undergo fission and fusion events that maintain a dynamic reticular network. Drp1 is a fundamental component of mitochondrial fission. Indeed, Drp1 deficient neurons have large, strongly interconnected mitochondria due to dysfunctional fission machinery. Fission helps facilitate mitophagy, which is the breakdown and r ...
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Binary Fission
Binary may refer to: Science and technology Mathematics * Binary number, a representation of numbers using only two digits (0 and 1) * Binary function, a function that takes two arguments * Binary operation, a mathematical operation that takes two arguments * Binary relation, a relation involving two elements * Binary-coded decimal, a method for encoding for decimal digits in binary sequences * Finger binary, a system for counting in binary numbers on the fingers of human hands Computing * Binary code, the digital representation of text and data * Bit, or binary digit, the basic unit of information in computers * Binary file, composed of something other than human-readable text ** Executable, a type of binary file that contains machine code for the computer to execute * Binary tree, a computer tree data structure in which each node has at most two children Astronomy * Binary star, a star system with two stars in it * Binary planet, two planetary bodies of comparable ...
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Mitochondrial Fusion
Mitochondria are dynamic organelles with the ability to fuse and divide ( fission), forming constantly changing tubular networks in most eukaryotic cells. These mitochondrial dynamics, first observed over a hundred years ago are important for the health of the cell, and defects in dynamics lead to genetic disorders. Through fusion, mitochondria can overcome the dangerous consequences of genetic malfunction. The process of mitochondrial fusion involves a variety of proteins that assist the cell throughout the series of events that form this process. Process overview When cells experience metabolic or environmental stresses, mitochondrial fusion and fission work to maintain functional mitochondria. An increase in fusion activity leads to mitochondrial elongation, whereas an increase in fission activity results in mitochondrial fragmentation. The components of this process can influence programmed cell death and lead to neurodegenerative disorders such as Parkinson's disease. Su ...
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Reactive Oxygen Species
In chemistry, reactive oxygen species (ROS) are highly reactive chemicals formed from diatomic oxygen (). Examples of ROS include peroxides, superoxide, hydroxyl radical, singlet oxygen, and alpha-oxygen. The reduction of molecular oxygen () produces superoxide (), which is the precursor to most other reactive oxygen species: :O2 + e^- -> \ ^\bullet O2- Dismutation of superoxide produces hydrogen peroxide (): :2 H+ + \ ^\bullet O2^- + \ ^\bullet O2^- -> H2O2 + O2 Hydrogen peroxide in turn may be partially reduced, thus forming hydroxide ions and hydroxyl radicals (), or fully reduced to water: :H2O2 + e^- -> HO^- + \ ^\bullet OH :2 H+ + 2 e- + H2O2 -> 2 H2O In a biological context, ROS are byproducts of the normal metabolism of oxygen. ROS have roles in cell signaling and homeostasis. ROS are intrinsic to cellular functioning, and are present at low and stationary levels in normal cells. In plants, ROS are involved in metabolic processes related to photoprotection and toleran ...
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Endoplasmic Reticulum
The endoplasmic reticulum (ER) is, in essence, the transportation system of the eukaryotic cell, and has many other important functions such as protein folding. It is a type of organelle made up of two subunits – rough endoplasmic reticulum (RER), and smooth endoplasmic reticulum (SER). The endoplasmic reticulum is found in most eukaryotic cells and forms an interconnected network of flattened, membrane-enclosed sacs known as cisternae (in the RER), and tubular structures in the SER. The membranes of the ER are continuous with the outer nuclear membrane. The endoplasmic reticulum is not found in red blood cells, or spermatozoa. The two types of ER share many of the same proteins and engage in certain common activities such as the synthesis of certain lipids and cholesterol. Different types of cells contain different ratios of the two types of ER depending on the activities of the cell. RER is found mainly toward the nucleus of cell and SER towards the cell membrane or plasma ...
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Calcineurin
Calcineurin (CaN) is a calcium and calmodulin dependent serine/threonine protein phosphatase (also known as protein phosphatase 3, and calcium-dependent serine-threonine phosphatase). It activates the T cells of the immune system and can be blocked by drugs. Calcineurin activates nuclear factor of activated T cell cytoplasmic (NFATc), a transcription factor, by dephosphorylating it. The activated NFATc is then translocated into the nucleus, where it upregulates the expression of interleukin 2 (IL-2), which, in turn, stimulates the growth and differentiation of the T cell response. Calcineurin is the target of a class of drugs called calcineurin inhibitors, which include ciclosporin, voclosporin, pimecrolimus and tacrolimus. Structure Calcineurin is a heterodimer of a 61-kD calmodulin-binding catalytic subunit, calcineurin A and a 19-kD Ca2+-binding regulatory subunit, calcineurin B. There are three isozymes of the catalytic subunit, each encoded by a separate gene (PPP3CA, ...
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Mitochondrial Fission Factor
Mitochondrial fission factor (Mff) is a protein that in humans is encoded by the ''MFF'' gene. Its primary role is in controlling the division of mitochondria. It has also been shown to regulate peroxisome morphology. Role in mitochondrial fission Mff is an outer mitochondrial membrane protein that binds to the GTPase GTPases are a large family of hydrolase enzymes that bind to the nucleotide guanosine triphosphate (GTP) and hydrolyze it to guanosine diphosphate (GDP). The GTP binding and hydrolysis takes place in the highly conserved P-loop "G domain", a pro ... Drp1; the Mff-Drp1 complex is what promotes mitochondrial fission. Knockdown of Mff causes the mitochondrial network to expand (by releasing the Drp1 foci from the outer mitochondrial membrane), while Mff overexpression causes it to become fragmented (by stimulating mitochondrial recruitment of Drp1). References Further reading * {{gene-2-stub Mitochondria ...
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Mitophagy
Mitophagy is the selective degradation of mitochondria by autophagy. It often occurs to defective mitochondria following damage or stress. The process of mitophagy was first described over a hundred years ago by Margaret Reed Lewis and Warren Harmon Lewis. Ashford and Porter used electron microscopy to observe mitochondrial fragments in liver lysosomes by 1962, and a 1977 report suggested that "mitochondria develop functional alterations which would activate autophagy." The term "mitophagy" was in use by 1998. Mitophagy is key in keeping the cell healthy. It promotes turnover of mitochondria and prevents accumulation of dysfunctional mitochondria which can lead to cellular degeneration. It is mediated by Atg32 (in yeast) and NIX and its regulator BNIP3 in mammals. Mitophagy is regulated by PINK1 and parkin proteins. In addition to the selective removal of damaged mitochondria, mitophagy is also required to adjust mitochondrial numbers to changing cellular metabolic needs, for stea ...
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Yeast
Yeasts are eukaryotic, single-celled microorganisms classified as members of the fungus kingdom. The first yeast originated hundreds of millions of years ago, and at least 1,500 species are currently recognized. They are estimated to constitute 1% of all described fungal species. Yeasts are unicellular organisms that evolved from multicellular ancestors, with some species having the ability to develop multicellular characteristics by forming strings of connected budding cells known as pseudohyphae or false hyphae. Yeast sizes vary greatly, depending on species and environment, typically measuring 3–4  µm in diameter, although some yeasts can grow to 40 µm in size. Most yeasts reproduce asexually by mitosis, and many do so by the asymmetric division process known as budding. With their single-celled growth habit, yeasts can be contrasted with molds, which grow hyphae. Fungal species that can take both forms (depending on temperature or other conditions) are ca ...
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Signal Transducing Adaptor Protein
Signal transducing adaptor proteins (STAPs) are proteins that are accessory to main proteins in a signal transduction pathway. Adaptor proteins contain a variety of protein-binding modules that link protein-binding partners together and facilitate the creation of larger signaling complexes. These proteins tend to lack any intrinsic enzymatic activity themselves, instead mediating specific protein–protein interactions that drive the formation of protein complexes. Examples of adaptor proteins include MYD88, Grb2 and SHC1. Signaling components Much of the specificity of signal transduction depends on the recruitment of several signalling components such as protein kinases and G-protein GTPases into short-lived active complexes in response to an activating signal such as a growth factor binding to its receptor. Domains Adaptor proteins usually contain several domains within their structure (e.g., Src homology 2 (SH2) and SH3 domains) that allow specific interactions with sev ...
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GTPases
GTPases are a large family of hydrolase enzymes that bind to the nucleotide guanosine triphosphate (GTP) and hydrolyze it to guanosine diphosphate (GDP). The GTP binding and hydrolysis takes place in the highly conserved P-loop "G domain", a protein domain common to many GTPases. Functions GTPases function as molecular switches or timers in many fundamental cellular processes. Examples of these roles include: * Signal transduction in response to activation of cell surface receptors, including transmembrane receptors such as those mediating taste, smell and vision. * Protein biosynthesis (a.k.a. translation) at the ribosome. * Regulation of cell differentiation, proliferation, division and movement. * Translocation of proteins through membranes. * Transport of vesicles within the cell, and vesicle-mediated secretion and uptake, through GTPase control of vesicle coat assembly. GTPases are active when bound to GTP and inactive when bound to GDP. In the generalized rece ...
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