IndraLab

Statements


AP180 binds CALM1. 13 / 13
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sparser
"The CALM and AP180 ANTH domains bind to cargo proteins in the VAMP family [ xref , xref , xref , xref , xref ]."

sparser
"In addition, recent results show that the ENTH (epsin NH2-terminal homology) domain [4] of epsin [5•] and the closely related ENTH-like domain of CALM [6••] and AP180 [7•] bind specifically to[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

sparser
"The ANTH domain represents an α-helical structure containing a lipid binding site which mediates the association of AP180 and CALM with PI(4,5)P 2 and therefore their membrane recruitment (Ford et al., xref )."

sparser
"AP180 and its ubiquitously expressed close paralog CALM ( Bushlin et al., 2008; Koo et al., 2011; Maritzen et al., 2012; Miller et al., 2011 ) directly interact with and facilitate endocytosis of Syb2[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

sparser
"Nevertheless, if AP180 and CALM are exclusively associated with the CCVs at the plasma membrane, one would expect to see the immunogold particles located in close proximity to the cell surface."

sparser
"This subfamily has limited homology with the Ub-binding region of the CALM-AP180 subfamily and residues that might coordinate Ub-binding in this ANTH subfamily were not obvious by sequence alignment alone."

sparser
"Biochemically, AP180 and CALM can bind to PtdIns(4,5)P 2 and clathrin simultaneously, enabling membrane tethering of clathrin."

sparser
"In addition to their pivotal function in recruiting the endocytic machinery, both AP180 and CALM bind to the N-terminal half of the Syb2 SNARE motif through their ANTH domain (Figure xref )."

sparser
"For Synaptobrevin2 this confinement was shown to depend on its interactions with its endocytic adaptors AP180 and CALM, presumably aided by a presynaptic diffusion barrier of unknown identity (Gimber et al., xref )."

sparser
"The association of Synaptobrevin2 with its adaptors AP180 and CALM or with Synaptophysin1 cannot facilitate the removal of cis-SNARE complexes since these interactions only work with non-SNARE-complexed Synaptobrevin2."

sparser
"Endocytic sorting of synaptobrevin 2 is mediated by direct interaction of the ANTH domain of the related endocytic adaptors CALM and AP180 with the N-terminal half of the SNARE motif centered around M46, as evidenced by NMR spectroscopy analysis and site-directed mutagenesis."

sparser
"Defective SNARE endocytosis may also underlie the association of CALM and AP180 with neurodevelopmental and cognitive defects or neurodegenerative disorders."

sparser
"We do not understand why LAP has the strongest interaction with vGlut in flies, whereas AP180 or CALM does not interact with vGlut in mammals."