Abstract
Coordination between different cytoskeletal systems is crucial for many cell biological functions, including cell migration and mitosis, and also plays an important role during tissue morphogenesis. Proteins of the class of cytoskeletal crosslinkers, or cytolinkers, have the ability to interact with more than one cytoskeletal system at a time and are prime candidates to mediate any coordination. One such class comprises the Gas2-like proteins, combining a conserved calponin-homology-type actin-binding domain and a Gas2 domain predicted to bind microtubules (MTs). This domain combination is also found in spectraplakins, huge cytolinkers that play important roles in many tissues in both invertebrates and vertebrates. Here, we dissect the ability of the single Drosophila Gas2-like protein Pigs to interact with both actin and MT cytoskeletons, both in vitro and in vivo, and illustrate complex regulatory interactions that determine the localisation of Pigs to and its effects on the cytoskeleton.
Highlights
The actin and microtubule (MT) cytoskeletons are important for many cell biological functions (Rodriguez et al, 2003)
Coexpression of GFP–PigsFL with mCherry–Tubulin confirmed that GFP–PigsFL was localised to the ends of MTs (Fig. 1B), and GFP–PigsFL partially colocalised with the plus-endtracking protein (+TIP) EB1–mRFP when coexpressed (Fig. 1C)
We found that GFP–PigsSxIP1/2/3mut partially colocalised with actin in Drosophila tissue culture cells (Fig. 8E), similar to GFP–PigsCH-Gas2b
Summary
The actin and microtubule (MT) cytoskeletons are important for many cell biological functions (Rodriguez et al, 2003) Both cytoskeletal networks have often been studied independently, and research has identified many factors that modulate the dynamic behaviour and structure of each system. Even though many accessory cytoskeletal proteins that remodel actin or MTs have been identified, only a few classes of proteins have been shown to be able to bind to both simultaneously and thereby crosslink and coordinate the two networks.
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