CRMP2, collapsin response mediator protein-2 ROS, reactive oxygen species. This modification of CRMP2 could promote microtubule remodeling, which along with actin remodeling promotes semaphorin-mediated growth cone collapse. The H 2O 2 produced by MICALs causes oxidation and dimerization of CRMP2, which then binds to thioredoxin (TRX) and is phosphorylated by GSK-3b. MICAL proteins regulate actin organization and on their loss, cytoskeletal organization is affected.
Actin filaments can also be altered indirectly by the H 2O 2 produced by MICAL proteins. MICAL proteins directly oxidize actin at methionine residues, causing depolymerization of actin filaments. On activation, and in the presence of NADPH, MICAL uses its FAD domain to either oxidize proteins or produce ROS such as H 2O 2. MICAL proteins are activated either on semaphorin signaling or by the binding of proteins that relieve their auto inhibition. Additional directions include expanding studies toward the MICAL-like homologs that lack flavin adenine dinucleotide domains and oxidation activity.Īctivation and function of MICAL proteins. The identification of additional substrates oxidized by MICAL will shed new light on MICAL protein function. It remains unclear whether MICAL proteins employ both mechanisms or whether the activity of MICAL-family proteins might vary with different substrates. MICAL proteins oxidize proteins through two mechanisms: either directly by oxidizing methionine residues or indirectly via the production of ROS. New York had the highest population of Mical families in 1840. This was 100 of all the recorded Micals in USA. In 1840 there were 2 Mical families living in New York. The most Mical families were found in USA in 1920. ROS production by MICALs also causes oxidation of collapsin response mediator protein-2, a microtubule assembly promoter, which subsequently undergoes phosphorylation. The Mical family name was found in the USA, the UK, and Scotland between 18. Recent studies show that MICALs directly induce oxidation of actin molecules, leading to actin depolymerization. This review describes the MICAL-family members, and discusses their mechanisms of actin-binding and regulation of actin cytoskeleton organization. Actin is one such protein that is affected by MICAL function, leading to dramatic cytoskeletal rearrangements. This mono-oxygenase domain generates redox potential with which MICALs can either oxidize proteins or produce reactive oxygen species (ROS). An interesting feature of MICAL proteins is the presence of an N-terminal flavo-mono-oxygenase domain.
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