This entry represents the N-terminal of human Calmodulin-regulated spectrin-associated protein 1-3 (CASAMP1-3, [, ]) and similar animal proteins, including the homologues from Caenorhabditis elegans [, , ]and Drosophila melanogaster [, , ]Patronin. This domain is a presumed calponin-homology (CH) domain.The calmodulin-regulated spectrin-associated (CAMSAP) proteins are defined by a CKK domain that binds microtubules []. It includes CAMSAPs from vertebrates and Patronin from invertebrates []. CAMSAP1 is the representative member. It contains a conserved region, CC1, that binds to both spectrin and Ca2+/calmodulin in vitro and links spectrin-binding to neurite outgrowth []. Patronin binds to and protects the MT minus-end against depolymerization []. CAMSAP2 is a key microtubule-organising protein that specifically binds the minus end of non-centrosomal microtubules and regulates their dynamics and organisation. CAMSAP proteins carry an N-terminal region that includes two CH domains represented by and , a central region including a predicted coiled-coil, and a C-terminal CKK domain , which is involved in binding CAMSAP proteins to microtubules [].
This entry represents the second Calponin-homology (CH) domain found in CAMSAP and related proteins from animals.The calmodulin-regulated spectrin-associated (CAMSAP) proteins are defined by a CKK domain that binds microtubules []. It includes CAMSAPs from vertebrates and Patronin from invertebrates []. CAMSAP1 is the representative member. It contains a conserved region, CC1, that binds to both spectrin and Ca2+/calmodulin in vitro and links spectrin-binding to neurite outgrowth []. Patronin binds to and protects the MT minus-end against depolymerization []. CAMSAP2 is a key microtubule-organising protein that specifically binds the minus end of non-centrosomal microtubules and regulates their dynamics and organisation. CAMSAP proteins carry an N-terminal region that includes two CH domains represented by and , a central region including a predicted coiled-coil, and a C-terminal CKK domain , which is involved in binding CAMSAP proteins to microtubules [].
The calmodulin-regulated spectrin-associated (CAMSAP) proteins are defined by a CKK domain that binds microtubules []. It includes CAMSAPs from vertebrates and Patronin from invertebrates []. CAMSAP1 is the representative member. It contains a conserved region, CC1, that binds to both spectrin and Ca2+/calmodulin in vitro and links spectrin-binding to neurite outgrowth []. Patronin binds to and protects the MT minus-end against depolymerization []. CAMSAP2 is a key microtubule-organising protein that specifically binds the minus end of non-centrosomal microtubules and regulates their dynamics and organisation. CAMSAP proteins carry an N-terminal region that includes two CH domains represented by and , a central region including a predicted coiled-coil, and a C-terminal CKK domain , which is involved in binding CAMSAP proteins to microtubules [].
The CKK domain occurs at the C-terminal in CAMSAP proteins. The structure of the CKK domain is a ��-barrel with an associated ��-helical hairpin. Characteristically, the CKK domain has a single invariant tryptophan residue within the core of the predicted ��-barrel. Residues that interact with this Trp to form part of this core are highly conserved too.The calmodulin-regulated spectrin-associated (CAMSAP) proteins are defined by a CKK domain that binds microtubules []. It includes CAMSAPs from vertebrates and Patronin from invertebrates []. CAMSAP1 is the representative member. It contains a conserved region, CC1, that binds to both spectrin and Ca2+/calmodulin in vitro and links spectrin-binding to neurite outgrowth []. Patronin binds to and protects the MT minus-end against depolymerization []. CAMSAP2 is a key microtubule-organising protein that specifically binds the minus end of non-centrosomal microtubules and regulates their dynamics and organisation. CAMSAP proteins carry an N-terminal region that includes two CH domains represented by and , a central region including a predicted coiled-coil, and a C-terminal CKK domain , which is involved in binding CAMSAP proteins to microtubules [].
This entry represents a conserved region found in calmodulin-regulated spectrin-associated proteins (CAMSAPs) from animals. This conserved region (also known as CC1 region) binds to both spectrin and Ca2+/calmodulin in vitro, although the binding of Ca2+/calmodulin inhibits the binding of spectrin. CC1 appears to be a functional region of CAMSAP1 that links spectrin-binding to neurite outgrowth [].The calmodulin-regulated spectrin-associated (CAMSAP) proteins are defined by a CKK domain that binds microtubules []. It includes CAMSAPs from vertebrates and Patronin from invertebrates []. CAMSAP1 is the representative member. It contains a conserved region, CC1, that binds to both spectrin and Ca2+/calmodulin in vitro and links spectrin-binding to neurite outgrowth []. Patronin binds to and protects the MT minus-end against depolymerization []. CAMSAP2 is a key microtubule-organising protein that specifically binds the minus end of non-centrosomal microtubules and regulates their dynamics and organisation. CAMSAP proteins carry an N-terminal region that includes two CH domains represented by and , a central region including a predicted coiled-coil, and a C-terminal CKK domain , which is involved in binding CAMSAP proteins to microtubules [].
This domain is found in human CDK5 regulatory subunit-associated protein 2 (CDK5RAP2), myomegalin (MYOME, also known as PDE4DIP) and related sequences mainly from vertebrates.CDK5RAP2 is a potential regulator of CDK5 activity that plays a role in the spindle checkpoint activation and regulates centrosomal maturation []. It plays a role in the spindle checkpoint activation by acting as a transcriptional regulator of both BUBR1 and MAD2 promoter. Together with EB1/MAPRE1, it may promote microtubule polymerization, bundle formation, growth and dynamics at the plus []. It forms a complex with MYOME isoform 13/MMG8/SMYLE, MAPRE1 and AKAP9, to contribute to microtubules nucleation and extension from the centrosome to the cell periphery []. MYOME participates in microtubule dynamics, promoting microtubule assembly. Depending upon the cell context, may act at the level of the Golgi apparatus or that of the centrosome [, , , ]. It forms a complex with AKAP9, and recruits CAMSAP2 to the Golgi apparatus and tethers non-centrosomal minus-end microtubules to the Golgi, an important step for polarised cell movement [, ].This entry represents a centrally located region that forms an ��-helical coiled-coil (CC) in these proteins.
