Fission yeast leucine-rich repeat protein Lrp1 is essential for cell morphogenesis as a component of the morphogenesis Orb6 network (MOR).

Biosci Biotechnol Biochem

Department of Molecular Biotechnology, Graduate School of Advanced Sciences of Matter, Hiroshima University, Kagamiyama, Higashi-hiroshima, Japan.

Published: December 2013

AI Article Synopsis

  • In fission yeast, cell morphogenesis is governed by the MOR network, which includes five conserved proteins essential for maintaining cell shape and successfully separating cells after division.
  • The study identifies Lrp1, a leucine-rich repeat protein, as a crucial new component of the MOR network needed for both cell growth and morphogenesis, functioning similarly to Sog2 in budding yeast.
  • Lrp1 is located at spindle pole bodies throughout the cell cycle and plays a vital role by interacting with Nak1 to activate Orb6 kinase, indicating its regulatory position in the cell morphogenesis process.

Article Abstract

In eukaryotes, cell morphogenesis is regulated coordinately with the cell cycle. In fission yeast, the morphogenesis network MOR (morphogenesis Orb6 network) consists of 5 conserved proteins, Pmo25, Nak1, Mor2, Orb6, and Mob2, and is essential for cell polarity control and cell separation following cytokinesis. Here we show that the conserved leucine-rich repeat protein Lrp1 is required for cell morphogenesis as a newly recognized component of MOR. Lrp1 has 4 leucine-rich repeats in its N-terminus and is a homolog of the budding yeast Sog2, which is a component of the RAM network (regulation of Ace2 activity and cellular morphogenesis). Lrp1 was essential for both cell growth and cell morphogenesis as were the other MOR components. Lrp1 was localized to the SPBs (spindle pole bodies, the yeast equivalent of the animal centrosome) throughout the cell cycle and to the medial ring during cytokinesis. Lrp1 interacted with Nak1 and was important for Orb6 kinase activity. Thus Lrp1 proved to function upstream of Orb6 in cell morphogenesis.

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Source
http://dx.doi.org/10.1271/bbb.130064DOI Listing

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