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Fig. 1. Phosphorylation sites detected in human GIT1. (A) Ser, Thr and Tyr coverage of the FLAG-GIT1 sequence (tag not shown) generated with trypsin. Detected tryptic peptides are bold and underlined. Residues not covered are shaded in gray. Observed phosphorylation sites are red. Red brackets above residues indicate that a phosphorylation site could not be located unambiguously to a specific amino acid. Ninety-six percent of the Ser, Thr and Tyr sites were covered. (B) Illustration of GIT1 with its domains. GIT1 contains a N-terminal ARF-GAP domain, ankyrin repeats (ANK), a Spa2 homology domain 1 (SHD1) and a C-terminal paxillin-binding domain. GIT1 localizes to synapses in hippocampal neurons via a newly described domain termed synaptic localization domain (SLD). Several signaling molecules, including focal adhesion kinase (FAK), p21-activated kinase interacting exchange factor (PIX), phospholipase C (PLC), mitogen-activated protein kinase kinase 1 (MEK1) and the synaptic protein Piccolo, associate with GIT1 through SHD (Haendeler et al., 2003 ; Kim et al., 2003; Yin et al., 2004; Zhao et al., 2000). The synaptic protein liprin- interacts with GIT1 through a region that includes part of the SLD and the C-terminus of GIT (Ko et al., 2003). Stars indicate the approximate locations of phosphorylation sites within the various protein domains.
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