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Cell (2007)_Allingham, Gilbert et al._Vik1, Kar3 by Mind Map: Cell (2007)_Allingham, Gilbert et
al._Vik1, Kar3
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Cell (2007)_Allingham, Gilbert et al._Vik1, Kar3


N-terminal region for cargo-binding

Role in karyogamy and vegetative growth

nuclear fusion event during mating

One of 6 kinesins in s. cerev.

only kinesin-14, motor domain is at c-term, minus-directed

Forms heterodimer in vivo

either cik1

or vik1 (vik1 not a motor)

Question: Should we not think of Kar3 as the "special" part of the heterodimer, but rather as a general motor adapter for proteins like cik1 or vik1?


In absence of vik1, localizes Kar3 along length of spindle


Localizes kar3 to spindle poles

similar to catalytic motor core of kinesin, but lacks ATP-binding site

At c-terminus, like kinesin-14s, For some reason, I noted this as important because of symmetry of coiled-coil (I guess I meant that it has to match it's partner in terms of which end it's at)

Kar3/Vik1 binds MT cooperatively and stabilizes MTs

They speculate that it may have evolved from common ancestor with kar3

Role at spindle is maybe to focus and crosslink MTs @ spindle

Has analagous neck region to NCD

Is it new information that it might bind MTs?

Skeptical of the 54% result


John. S. Allingham

U. Wisconsin

Lisa R. Sproul


Ivan Rayment

U. Wisconsin

Susan P. Gilbert

Pitt (now RPI)

In kinesins, nucleotide binding pocket is highly conserved

NCD may only bind with one head

Other Questions that occurred to me

What would happen if make fusion protein of dimer of kinesin 14 and kinesin-1? (not chimeric monomers, but each motor linked by a flexible linker perhaps)

What about expressing kinesin-1 dimers?

I believe it was the Diehl lab at the 2010 Biophys Meeting that showed this (think they've been doing it a while)...the kinesin "scaffolds", 1924-POS BOARD #B722 MULTIPLE INTERACTING KINESIN-1 MOTORS COOPERATE NEGATIVELY. Michael R. Diehl, D. Kenneth Jameson, Mathew Zimmerman, Jonathan D. Driver, Arthur R. Rogers.