The CRP/MLP/TLP family of LIM domain proteins: Acting by connecting

Abstract

In vertebrates, members of the cysteine-rich protein (CRP) family are characterized by the presence of two LIM domains linked to short glycine-rich repeats. These proteins mediate protein-protein interactions and are of fundamental importance for cell differentiation, cytoskeletal remodeling, and transcriptional regulation. To date, a vast amount of information about vertebrate CRPs has become available, including their biological functions, interacting partners, and three-dimensional structures. Compatible with a molecular adapter role, structural data reveal that the LIM domains within these proteins represent completely independent folded units bridged by flexible linker regions. The physiological roles for individual CRPs was determined by targeted gene disruption analysis and by identification of common and specific binding partners by means of yeast and mammalian two-hybrid screens. Several CRP-like LIM domain proteins with close structural and sequence similarity were identified in arthropods, protozoas and plants, supporting the notion that this subset of LIM domain proteins has been highly conserved over the span of evolution thereby emphasizing the importance of their function.

Quantitative Proteomics of a Presymptomatic A53T α-Synuclein Drosophila Model of Parkinson Disease

“…Muscle LIM protein at 60A (Mlp60A) was up-regulated in A53T ␣-synuclein-expressing flies relative to controls (Table II). Mlp60A is a member of the cysteine-rich protein family that plays pivotal roles in cell differentiation (55). Mlp60A is associated with the actin cytoskeleton and plays a role in myogenic differentiation (56,57).…”

Mouse Prickle1 and Prickle2 are expressed in postmitotic neurons and promote neurite outgrowth

“…The total RNA extract was reverse transcribed by using oligo(dT) [12][13][14][15][16][17][18] 0 (reverse complement of bases 1833-1852). Serial sagittal sections that were 14-lm thick were prepared and thaw-mounted on Matsunami Adhesive Silane (MAS)-coated glass slides (Matsunami Glass Ind., Osaka, Japan).…”

“…However, no information is available regarding the involvement of the mouse Prickle genes in brain function both in the late embryonic and mature stages. Besides the Drosophila and Xenopus prickle proteins, the mouse Prickle1 and Prickle2 proteins also have conserved three cysteine-rich sequences with a double zinc-finger motif (LIM) domain, which is known to play important roles in the fundamental biological processes that occur during embryonic stages [1,[16][17][18][19]. Recently, candidate functions of the PCP gene family in the late embryonic stages have been reported.…”

The plant LIM proteins: unlocking the hidden attractions

“…The information in response to 2LIMs under stress hormone will also be helpful to identify the mechanism or metabolism related to stress conditions. Moreover, as this domain was itself identified as protein-protein interaction module (Zheng and Zhao 2007;Weiskirchen and Günther 2003), chances of its interaction with other proteins and thus their subsequent networking also need special consideration. One such example, recently came from rice, where LIM domain proteins were shown to interact with other proteins (Na et al 2014), yet their authenticity and exact biological relevance were not much addressed and thus require further experimentation.…”