1 eceptor, SH3 domains, phosphoinositides, and beta-adaptin.

2 ound in xARH abolished binding to alpha- and beta-adaptins.

3 n correlates with increased interaction with beta-adaptin, a subunit of the clathrin adaptor protein

4  receptor internalization and bind clathrin, beta-adaptin, and Src to comparable levels as wild type

5 ion; beta-arrestins contain clathrin adaptor beta-adaptin-binding sites, whereas alpha-arrestins harb

6 s of the endocytic syntaxins, Rab 5, and the beta-adaptins each reveal a pattern of ancestral, undiff

7 ed LLNLD clathrin box motif derived from the beta-adaptin hinge region.

8  in vitro with beta-NAP, a neuronal-specific beta-adaptin homolog that was identified as an autoantig

9  data describing the association of ATM with beta-adaptin in vesicles indicate that ATM may play a ro

10 minant-negative mutants lacking clathrin- or beta-adaptin interaction sites fails to block GPER inter

11              CD63, clathrin heavy chain, and beta-adaptin mRNAs, all of which encode proteins associa

12 ataxia telangiectasia mutated (ATM) binds to beta-adaptin, one of the components of the AP-2 adaptor

13 gulate interaction with endocytic (clathrin, beta-adaptin) or signaling (Src) components and is in co

14 arrestin motifs recognizing clathrin and the beta-adaptin subunit of AP2.

15 f Nef bound directly and specifically to the beta-adaptin subunit of the clathrin adaptor complexes A

16 ns from embryo extracts including alpha- and beta-adaptins, subunits of the AP-2 endocytic complex.

17 g of beta-arrestin 2 to clathrin heavy chain/beta-adaptin, thereby accelerating receptor internalizat

18                                          For beta-adaptins, this fragment binds to cytoplasmic di-leu

19              The interaction between ATM and beta-adaptin was confirmed in vitro, and coimmunoprecipi