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A S mall P eptide S equence is S ufficient for I nitiating K inesin‐1 A ctivation T hrough P art of TPR R egion of KLC1
Author(s) -
Kawano Takanori,
Araseki Masahiko,
Araki Yoichi,
Kinjo Masataka,
Yamamoto Tohru,
Suzuki Toshiharu
Publication year - 2012
Publication title -
traffic
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.677
H-Index - 130
eISSN - 1600-0854
pISSN - 1398-9219
DOI - 10.1111/j.1600-0854.2012.01350.x
Subject(s) - kinesin , tetratricopeptide , microbiology and biotechnology , motor protein , protein subunit , cytoplasm , biology , transport protein , microtubule , biochemistry , chemistry , gene
Kinesin‐1 anterogradely transports vesicles containing cargo proteins when a protein–protein interaction activates it from an inhibited state. The C ‐terminal cytoplasmic region of kinesin‐1 cargo protein A lcadeinα ( Alcα ) interacts with the KLC1 subunit's tetratricopeptide repeat ( TPR ) region, activating kinesin‐1's association with vesicles and anterograde transport. We found that either of two 10‐amino‐acid WD motifs in Alcα cytoplasmic region was necessary and sufficient to initiate this activation. An artificial transmembrane protein containing either WD motif induced kinesin‐1's vesicular association and anterograde transport in a KLC ‐dependent manner, even in the normally inhibiting presence of excess KLC1 , thus allowing us to analyze the KLC1 TPR‐WD functional interaction in detail in vivo . A part of TPR region was dispensable for the WD motifs' activation of kinesin‐1 and transport, indicating that only part of the TPR structure is required for this function in vivo . For a different kinesin‐1 cargo protein, JIP1 , an 11‐amino‐acid C ‐terminal region was sufficient to recruit KLC1 to vesicles, but did not activate transport. These observations suggest that structurally different TPR ‐interacting peptides may have different effects on kinesin‐1. This mechanism may partly explain how kinesin‐1 can organize the transport of a wide variety of cargo molecules.