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Colin Dingwall coauthored experiments identifying a protein domain that directs nucleoplasmin into the cell nucleus. Comparing fragments and injection locations separates nuclear import from simple retention after entry.

A domain can provide localization information without being the whole protein. Testing both cytoplasmic and nuclear placement helps distinguish a targeting signal from a feature that merely prevents export.^[ref]

A coauthor of the 1982 study of nucleoplasmin import through the nuclear pore complex.

In a 1982 experiment, purified nucleoplasmin was labeled with radioactive iodine and cleaved by proteolysis. Microinjection delivered cargo into Xenopus laevis oocyte cytoplasm. Manually separated cell nuclei and cytoplasm were compared by gel electrophoresis and autoradiography; section autoradiography checked internal localization. Tail-bearing cargo entered the cell nucleus; tailless cores did not. Direct nuclear microinjection retained the cores: the tails mattered for entry, but the assay did not identify a receptor.^[ref]

Direct nuclear microinjection bypassed entry, distinguishing failure to enter from failure to remain inside a cell nucleus.

Nucleoplasmin is a nuclear protein used in the nuclear pore localization experiment.

Its targeting information helped establish that a protein sequence can direct selective nuclear accumulation. Nuclear localization can therefore be tested by comparing intact and altered targeting sequences rather than inferring transport from protein size alone. ^[ref]

Researcher in intracellular protein targeting. Laskey coauthored experiments identifying a nucleoplasmin region that directs nuclear import, connecting a part of a protein with transport through the nuclear pore complex.^[ref]

Coauthor of experiments identifying a nucleoplasmin region that specifies migration into the cell nucleus. The study connected a defined part of a protein with selective nuclear targeting; the documented initials are retained without an unverified full-name expansion.^[ref]