High impact information on LLGL2

• The C-terminal tail of Lgl2 bound to LGN with a K(d) value of about 56 nm [1].
• Overexpression of the C-terminal tail of Lgl2 induced mis-localization of the nuclear mitotic apparatus protein NuMA and disorganization of the mitotic spindle during mitosis, eventually causing formation of multiple micronuclei [1].
• Direct binding of Lgl2 to LGN during mitosis and its requirement for normal cell division [1].
• These results indicate that Lgl2 forms a Lgl2.Par-6.aPKC.LGN complex, which responds to mitotic signaling to establish normal cell division [1].
• A comparison of lgl2 protein to sequences in the genome database suggested that lgl2 is a nuclear transport receptor [2].

Biological context of LLGL2

• 2. Comparison with sequences in the genome database identified lgl2 as a member of the karyopherin-beta family of nuclear import proteins, with greatest homology to transportin SR [3].
• We mapped LGL2 to chromosome 1p33-34 [3].
• Mean HGL output was 115 +/- 43 microg for 3 h and the overall intragastric lipolysis was 6.1 +/- 2.6% [4].

Anatomical context of LLGL2

• Northern analysis confirmed that LGL2 is differentially expressed in fetal lung (maximal during the pseudoglandular stage, gestational Days 14 to 16), induced by glucocorticoid, and enriched in epithelium relative to the mesenchyme [3].
• Intragastric fat digestion was investigated by analyzing the products of lipolysis and the gastric lipase (HGL) levels of premature infants fed with a formula enriched with medium chain triglycerides (MCT) and those of infants fed with human milk [4].
• On the basis of these data, LGL1 and 3 seem to be closely related to peripheral blood mature natural killer (NK) cells, whereas LGL2 displays a pattern of TCR and CD3 expression similar to that found in CD1-2-3-4-8-16-thymocytes [5].

References