Synonyms for heteromultimers or Related words with heteromultimers
Examples of "heteromultimers"
This gene encodes a protein for a voltage-gated potassium channel required for the repolarization phase of the cardiac action potential. The gene product can form
with two other potassium channel proteins, KCNE1 and KCNE3. The gene is located in a region of chromosome 11 that contains a large number of contiguous genes that are abnormally imprinted in cancer and the Beckwith-Wiedemann syndrome. Two alternative transcripts encoding distinct isoforms have been described.
Both KCC2 isoforms can form homomultimers, or
with other K-Cl symporters on the cell membrane to maintain chloride homeostasis in neurons. Dimers, trimers, and tetramers involving KCC2 have been identified in brainstem neurons. Oligomerization may play an important role in transporter function and activation, as it has been observed that the oligomer to monomer ratio increases in correlation to the development of the chloride ion gradient in neurons.
Proteins with different numbers of polyhistidine tags elute differently from nickel-affinity resin. For proteins with a single hexahistidine tag, 75 mM imidazole enables elution from Ni-NTA, whereas for proteins with two hexahistidine tags, 100 mM imidazole is required for elution. This step-wise elution may be used to isolate specific protein assemblies from a mixture, such as defined
(e.g. an AB heterodimer from a mixture including AA and BB homodimers, if only subunit B has a polyhistidine tag). Such an approach was used in isolation of monovalent streptavidin.
Voltage-gated potassium channels form the largest and most diversified class of ion channels and are present in both excitable and nonexcitable cells. Their main functions are associated with the regulation of the resting membrane potential and the control of the shape and frequency of action potentials. The alpha subunits are of 2 types: those that are functional by themselves and those that are electrically silent but capable of modulating the activity of specific functional alpha subunits. The protein encoded by this gene is not functional by itself but can form
with member 1 and with member 2 (and possibly other members) of the Shab-related subfamily of potassium voltage-gated channel proteins. This gene belongs to the S subfamily of the potassium channel family.
Acid-sensing ion channels (ASICs) are neuronal voltage-insensitive sodium channels activated by extracellular protons. ASIC proteins are a subfamily of the ENaC/Deg superfamily of ion channels. In mammalian genomes, the ASIC is encoded by five genes, ASIC1, ASIC2, ASIC3, ASIC4, and ASIC5. These genes have splice variants that encode for several isoforms that are marked by a suffix. For example, two major products of ASIC1 gene are called as ASIC1a and ASIC1b. ASICs are trimeric and can be made up of different combinations of subunits. ASIC2b is non-functional on its own but modulates channel activity when participating in
. ASIC4 has no known function. All ASICs are expressed in the peripheral nervous system while ASIC1a, 2a, 2b, 3 and 4 are expressed in the central nervous system. ASICs are Na permeable with ASIC1a showing low Ca permeability.
The four GIRK subunits are 80-90% similar in their pore-forming and transmembrane domains, a feature accountable by the similarities in their structures and sequences. GIRK2, GIRK3, and GIRK4 share an overall identity of 62% with each other, while GIRK1 only shares 44% identity with the others. Because of their similarity, the GIRK channel subunits can come together easily to form
(a protein with two or more different polypeptide chains). GIRK1, GIRK2, and GIRK3 show abundant and overlapping distribution in the central nervous system (CNS) while GIRK1 and GIRK4 are found primarily in the heart. GIRK1 combines with GIRK2 in the CNS and GIRK4 in the atrium to form heterotetramers; each final heterotetramer contains two GIRK1 subunits and two GIRK2 or GIRK4 subunits. GIRK2 subunits can also form homotetramers in the brain, while GIRK4 subunits can form homotetramers in the heart. GIRK1 subunits have not been shown to be able to form functional homotetramers. Though GIRK3 subunits are found in the CNS, their role in forming functional ion channels is still unknown.
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