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Kinesin, The Workhorse of the Living Cell
Author(s) -
Blythe Justin,
Burns Morgan,
Fuchs Kelsey,
Uttley Zach
Publication year - 2017
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.31.1_supplement.lb258
Subject(s) - kinesin , microtubule , coiled coil , molecular motor , motor protein , microbiology and biotechnology , biology , biophysics
For a living cell to stay vital, it must transport molecules and organelles to their designated positions within the cell. Similar to motorized interstate transport systems, cells achieve their transport using motor proteins. One fascinating motor protein, kinesin, hauls its cargo on microtubule tracks at a speed of 2 μm/sec, a process fueled by ATP hydrolysis. The structure of kinesin consists of two heads (motors) each with an ATP binding pocket and a microtubule‐binding domain that spans the length of its motor subunit. The two motors are attached to the neck domain, which consists of a neck linker and a neck coil. As it begins its journey, kinesin docks one motor head at a time to a microtubule unit. ATP binds to the docked head (the leading head) and undergoes hydrolysis, causing a power stroke. Detailed studies showed that this sequence of events leads to a kinesin's hand‐over‐hand moving pattern. Other structural elements in kinesin include a coiled‐coil stalk with hinge regions that allow kinesin to fold on itself, an energy saving process adopted when the protein is idle, a tail domain and a light chain subunit that contain cargo binding sites. Mutated kinesin has been linked to multiple diseases including, Alzheimer's, neurofibromatosis, Huntington's disease and cancer. The Pittsburg High School SMART TEAM used 3D technology to design a model of kinesin's motor and neck domains to better understand their structure‐function link. This knowledge may shed light on how mutations in these regions can lead to diseases linked to kinesin's role in cellular transport.