Integral membrane proteins of the nuclear envelope interact with lamins and chromosomes, and binding is modulated by mitotic phosphorylation

Article Abstract:

In vitro assays demonstrate that lamino-associated polypeptides (LAPs), 1A and 1B in particular, bind to lamins A and C and B, but LAP 2 relates with lamin B and binds to mitotic chromosomes. LAP 2 may be crucial to the early processes in nuclear envelope reorganization, and LAP 2 and LAP 1 may be concerned with linking lamino to the nuclear envelope. Before the organization of a majority of lamins, during late anaphase, LAP 2 relates with chromosomes. LAPs 1A, 1B, 1C and 2 are integral membrane proteins of the nuclear envelope related to the nuclear lamina.

Influence, Observations, Eukaryotic cells, Cells (Biology), Eukaryotes, Phosphorylation

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A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2

Article Abstract:

SUMO-1, a novel peptide of 101 amino acids, has been found to be covalently linked to the mammalian Ran GTPase-activating protein RanGAP1 in an adenosine triphosphate-dependent reaction. SUMO-1 exhibits a homology to ubiquitin, a 76-residue protein found in eukaryotes. Data indicate that the polypeptide is involved in protein targeting and not degradation. At least three additional intranuclear proteins are modified with SUMO-1 or with a protein closely resembling it.

Research, Ubiquitin

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Nuclear export signals and the fast track to the cytoplasm

Article Abstract:

Not much research on nuclear export has been done. An analysis of the cAMP-dependent protein kinase and Rev, that rapidly shuttle between the nucleus and cytoplasm and having the potential to bear nuclear export signals (NESs) as well as import signals shows that short protein sequences are responsible for the rapid nuclear export. The shuttling species include RNA binding proteins as well as transcriptional activators and hsc70.

Signal peptides, Amino acid sequence, Amino acid sequencing

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