{"product_id":"filamin-a-scaffolding-protein-von-sarah-annesley","title":"Filamin: a scaffolding protein","description":"\u003cp\u003eFilamin is an actin-binding protein known to be  essential for wild type slug phototaxis in D.  discoideum. The protein contains an actin-binding  domain (ABD) followed by a rod domain containing 6  closely related repeat segments. Here I show that  repeats 2-6 in the rod domain and the ABD are  essential for wild type phototaxis, suggesting that  when these segments are missing proteins which bind  to these segments are excluded from the photosensory  pathway and phototaxis is impaired. Repeat 1 was  shown not to be essential if filamin¿1 was  overexpressed to levels 10X higher than wild type  filamin. This indicates that repeat 1 is not  involved in directly binding proteins but is still  required for the formation of fully functional  complexes. Coimmunoprecipitation experiments  identified 5 filamin-interacting proteins-RasD,  Erkb, AMPK, PKB \u0026amp; GRP125. The interaction with RasD  did not rely on a single repeat in the rod domain  nor the ABD. It is unknown how filamin interacts  with the other proteins involved in phototaxis but  it''s probable that filamin acts as a scaffold for  the assembly of a photosensory signalling complex  through its repeats, predominantly repeats 2-6.\u003c\/p\u003e\u003cdiv class=\"aw-variant-hidden-subtitle-div\" id=\"aw-variant-subtitle-9783838307411\"\u003e\u003ch3\u003eFilamin''s role as a scaffolding protein in a photosensory signalling complex in Dictyostelium discoideum\u003c\/h3\u003e\u003c\/div\u003e","brand":"Autorenwelt Shop","offers":[{"title":"Softcover - 9783838307411","offer_id":39497063006301,"sku":"9783838307411","price":79.0,"currency_code":"EUR","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0940\/0622\/files\/44d2488b-281e-4087-817e-4ea4bdad98f7.jpg?v=1757655707","url":"https:\/\/shop.autorenwelt.de\/products\/filamin-a-scaffolding-protein-von-sarah-annesley","provider":"Autorenwelt Shop","version":"1.0","type":"link"}