A Small Peptide Sequence is Sufficient for Initiating Kinesin-1 Activation Through Part of TPR Region of KLC1

作者：Kawano Takanori; Araseki Masahiko; Araki Yoichi; Kinjo Masataka; Yamamoto Tohru^*; Suzuki Toshiharu

来源：Traffic, 2012, 13(6): 834-848.

DOI：10.1111/j.1600-0854.2012.01350.x

• Alcadein
• calsyntenin
• JIP1
• kinesin-1
• KLC
• tetratricopeptide repeat

Kinesin-1 anterogradely transports vesicles containing cargo proteins when a proteinprotein interaction activates it from an inhibited state. The C-terminal cytoplasmic region of kinesin-1 cargo protein Alcadeina (Alca) interacts with the KLC1 subunit%26apos;s tetratricopeptide repeat (TPR) region, activating kinesin-1%26apos;s association with vesicles and anterograde transport. We found that either of two 10-amino-acid WD motifs in Alca cytoplasmic region was necessary and sufficient to initiate this activation. An artificial transmembrane protein containing either WD motif induced kinesin-1%26apos;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%26apos; 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.

• 出版日期2012-6