15-angstrom resolution model of the monomeric kinesin motor, KIF1A

Article Abstract:

K loop-microtubule (MT) interaction, mutant analysis and high-resolution cryo-electron microscopy (EM) have been used to study various questions about the cell and kinesin superfamily proteins and the usual two-headed structure believed to be needed for the kinesin molecular motor to move processively on the microtubule track. A 15-angstrom resolution structure clearly docked with the available atomic models showed the K loop to be an extra microtubule-binding domain specific to KIF1A and bound to the C terminus of tubulin. A motor domain construct of KIF1A, C351, is a monomeric protein with the first methionine in the middle of the sixth alpha helix in the motor domain and the 'neck-linker' of kinesin.

Usage, Cytochemistry, Neurons, Electron microscopy, Binding sites (Biochemistry), Active sites (Biochemistry), Tubulins, Cryobiochemistry, Tubulin

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A novel motor, KIF13A, transports mannose-6-phosphate receptor to plasma membrane through direct interaction with AP-1 complex

Article Abstract:

Research reveals that motor protein KIF13A is a member of of the kinesin superfamily proteins that exhibits microtubule-dependency cargoeing adaptor complex AP-1 and mannose-6-phosphate receptor. Data indicate that the protein targets the receptor containing vesciles from trans-Golgi network to plasma membrane.

Biological transport, Active, Active biological transport, Cell interaction, Cell interactions, Molecular neurobiology

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Kinesin superfamily protein 2A (KIF2A) functions in suppression of collateral branch extension

Article Abstract:

Research has been conducted on kinesin superfamily protein 2A. The authors suggest that this protein regulates microtubule dynamics at the growth cone edge via depolymerization of these microtubules, and that it is important for the collateral branch extension suppression.

Analysis, Genetic aspects, Cells (Biology), Growth, Proteins, Genetic regulation, Cells, Cell research, Cytological research, Company growth

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