MARK4 is a novel microtubule-associated proteins/microtubule affinity-regulating kinase that binds to the cellular microtubule network and to centrosomes.
AuthorsTrinczek B, Brajenovic M, Ebneth A, Drewes G,
JournalJ Biol Chem
PubMed ID14594945
The MARK protein kinases were originally identified by their ability to phosphorylate a serine motif in the microtubule-binding domain of tau that is critical for microtubule binding. Here, we report the cloning and expression of a novel human paralog, MARK4, which shares 75% overall homology with MARK1-3 and is predominantly ... More
Calpain 3 is activated through autolysis within the active site and lyses sarcomeric and sarcolemmal components.
AuthorsTaveau M, Bourg N, Sillon G, Roudaut C, Bartoli M, Richard I,
JournalMol Cell Biol
PubMed ID14645524
Calpain 3 (Capn3) is known as the skeletal muscle-specific member of the calpains, a family of intracellular nonlysosomal cysteine proteases. This enigmatic protease has many unique features among the calpain family and, importantly, mutations in Capn3 have been shown to be responsible for limb girdle muscular dystrophy type 2A. Here ... More
Serinc, an activity-regulated protein family, incorporates serine into membrane lipid synthesis.
AuthorsInuzuka M, Hayakawa M, Ingi T,
JournalJ Biol Chem
PubMed ID16120614
Cell membranes contain various transporter proteins, some of which are responsible for transferring amino acids across membrane. In this study, we report another class of carrier proteins, termed Serinc1-5, that incorporates a polar amino acid serine into membranes and facilitates the synthesis of two serine-derived lipids, phosphatidylserine and sphingolipids. Serinc ... More