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FERM domain C-lobe of Kinesin-like calmodulin binding protein KCBPs (also called KIPK/Kinesin-like Calmodulin-Binding Protein-Interacting Protein Kinase), a member of the Kinesin-14 family, is a C-terminal microtubule motor with three unique domains including a myosin tail homology region 4 (MyTH4), a talin-like domain, and a calmodulin-binding domain (CBD). Binding of the Ca2+-activated calmodulin to KCBP causes the motor to dissociate from microtubules. The microtubule binding of KCBP is controlled by the calcium binding protein KIC containing a single EF-hand motif. KCBPs are unique to land plants and green algae. The MyTH4 and talin-like domains are not found in other kinesins, while the CBD domain is also only found in Strongylocentrotus purpuratus kinesin-C (SpKinC). The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites. |
Jiyao W et al.(2023). "The conserved domain database in 2023.",